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Information on EC 1.3.5.1 - succinate dehydrogenase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8LBZ7

for references in articles please use BRENDA:EC1.3.5.1
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EC Tree
IUBMB Comments
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively. Under aerobic conditions the enzyme catalyses succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II). Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor. The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit. These enzymes catalyse an electrogenic reaction and are thus classified as EC 7.1.1.12, succinate dehydrogenase (electrogenic, proton-motive force generating).
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Arabidopsis thaliana
UNIPROT: Q8LBZ7
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
succinate dehydrogenase, complex ii, succinic dehydrogenase, mitochondrial complex ii, succinate dehydrogenase complex, mitochondrial succinate dehydrogenase, succinate dehydrogenase subunit b, succinate dehydrogenase b, sdhcdab, succinate-ubiquinone oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
complex II
-
-
-
-
dehydrogenase, succinate
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-
-
-
Fcc3
-
-
-
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FL cyt
-
-
-
-
Flavocytochrome c3
-
-
-
-
FRD
-
-
-
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fumarate reductase
-
-
-
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fumarate reductase complex
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-
-
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fumaric hydrogenase
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-
-
-
Ifc3
-
-
-
-
Iron(III)-induced flavocytochrome C3
-
-
-
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menaquinol-fumarate oxidoreductase
-
-
-
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menaquinol:fumarate oxidoreductase
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-
-
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succinate dehydrogenase (quinone)
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-
-
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succinate dehydrogenase complex
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-
-
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succinate oxidoreductase
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-
-
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succinate-coenzyme Q reductase
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-
-
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succinic acid dehydrogenase
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-
-
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succinic dehydrogenase
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-
-
-
succinodehydrogenase
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-
-
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succinyl dehydrogenase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively. Under aerobic conditions the enzyme catalyses succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II). Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor. The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit. These enzymes catalyse an electrogenic reaction and are thus classified as EC 7.1.1.12, succinate dehydrogenase (electrogenic, proton-motive force generating).
CAS REGISTRY NUMBER
COMMENTARY hide
9002-02-2
-
9028-11-9
-
9076-99-7
cf EC 1.3.1.6
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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flavinylation of SDH is dependent on SDH1:SDHA F2 interaction requiring the C-terminal tail of SDH1
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
transition from darkness to light causes a short transient increase in the SDH activity followed by a decrease to a half of the original activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protein SDHA F2
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the factor is needed for assembly and activity of SDH and also for normal root elongation, sequence diversity and conservation of SDHA F2 across kingdoms, phylogenetic analysis, overview
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additional information
-
transition from darkness to light causes a short transient increase in the SDH activity followed by a decrease to a half of the original activity
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression
Manually annotated by BRENDA team
additional information
-
the pattern of SDH activity is consistent in general with the pattern of expression of the genes sdh2-3 and to a lesser extent of sdh1-2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SDHB1_ARATH
279
0
31171
Swiss-Prot
Mitochondrion (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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the enzyme complex consits of four subunits: a flavoprotein SDH1, an iron-sulfur protein SDH2, two integral membrane subunits SDH3 and SDH4. Protein SDHA F2 is needed for assembly and activity of SDH and also for normal root elongation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Elorza, A.; Leon, G.; Gomez, I.; Mouras, A.; Holuigue, L.; Araya, A.; Jordana, X.
Nuclear SDH2-1 and SDH2-2 genes, encoding the iron-sulfur subunit of mitochondrial complex II in Arabidopsis, have distinct cell-specific expression patterns and promoter activities
Plant Physiol.
136
4072-4087
2004
Arabidopsis thaliana (Q8LB02), Arabidopsis thaliana (Q8LBZ7)
Manually annotated by BRENDA team
Popov, V.N.; Eprintsev, A.T.; Fedorin, D.N.; Igamberdiev, A.U.
Succinate dehydrogenase in Arabidopsis thaliana is regulated by light via phytochrome A
FEBS Lett.
584
199-202
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Huang, S.; Millar, A.
Sequence diversity and conservation in factors influencing succinate dehydrogenase flavinylation
Plant Signal. Behav.
8
e22815
2013
Arabidopsis thaliana
Manually annotated by BRENDA team