KEGG   ENZYME: 1.3.5.1Help
Entry
EC 1.3.5.1                  Enzyme                                 

Name
succinate dehydrogenase (quinone);
succinate dehydrogenase (ubiquinone);
succinic dehydrogenase;
complex II (ambiguous);
succinate dehydrogenase complex;
SDH;
succinate:ubiquinone oxidoreductase
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With a quinone or related compound as acceptor
BRITE hierarchy
Sysname
succinate:quinone oxidoreductase
Reaction(IUBMB)
succinate + a quinone = fumarate + a quinol [RN:R02164]
Reaction(KEGG)
Substrate
succinate [CPD:C00042];
quinone [CPD:C00472]
Product
fumarate [CPD:C00122];
quinol [CPD:C00530]
Comment
A flavoprotein (FAD) 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 and archaea. 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 utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone).
History
EC 1.3.5.1 created 1983
Pathway
Citrate cycle (TCA cycle)
Oxidative phosphorylation
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00234  
succinate dehydrogenase (ubiquinone) flavoprotein subunit
K00235  
succinate dehydrogenase (ubiquinone) iron-sulfur subunit
Genes
HSA: 
6389(SDHA) 6390(SDHB)
PTR: 
100608629(SDHA) 456526(SDHB) 750143(SDHA)
PPS: 
100987473(SDHA) 100989574(SDHB)
GGO: 
101131972(SDHB) 101141874(SDHA)
PON: 
100173631(SDHA) 100437700(SDHB)
MCC: 
MCF: 
MMU: 
66945(Sdha) 67680(Sdhb)
RNO: 
157074(Sdha) 298596(Sdhb)
CGE: 
HGL: 
101697591(Sdha) 101720891(Sdhb)
TUP: 
102480936(SDHB) 102502720(SDHA)
CFA: 
478217(SDHB) 478634(SDHA)
AML: 
FCA: 
751617(SDHB) 751619(SDHA)
BTA: 
281480(SDHA) 286840(SDHB)
BOM: 
102274978(SDHB) 102278228(SDHA)
PHD: 
102315900(SDHB) 102332015(SDHA)
CHX: 
102183107(SDHA) 102183195(SDHB)
SSC: 
414412(SDHB) 780433(SDHA)
CFR: 
102523856(SDHA) 102524547(SDHB)
ECB: 
100034244(SDHA) 100050091(SDHB)
MYB: 
MDO: 
751078(SDHB) 751085(SDHA)
SHR: 
100924299(SDHB) 100931806(SDHA)
OAA: 
GGA: 
100859720(SDHB) 395758(SDHA)
MGP: 
TGU: 
FAB: 
PHI: 
102108670(SDHA) 102114745(SDHB)
APLA: 
101792265(SDHA) 101793933(SDHB)
FPG: 
101916111(SDHA) 101918141(SDHB)
FCH: 
102047150(SDHB) 102047706(SDHA)
CLV: 
102092002(SDHB) 102093871(SDHA)
ASN: 
102372796(SDHA) 102373063(SDHB)
PSS: 
102445790(SDHB) 102455030(SDHA)
ACS: 
XLA: 
379939(sdhb) 380463(sdha) 398946(MGC68518)
XTR: 
100144957(sdhb) 548743(sdha)
DRE: 
393884(sdha) 562149(sdhb)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
550667(SdhA) 551169(GB14832)
NVI: 
100116862(SdhB) 100119074(Sdha)
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_C03G5.1(sdha-1) CELE_C34B2.7(sdha-2) CELE_F42A8.2(sdhb-1)
CBR: 
CBG00872(Cbr-sdhb-1) CBG12805(Cbr-sdha-2) CBG22795(Cbr-sdha-1)
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT2G18450(SDH1-2) AT3G27380(SDH2-1) AT5G40650(SDH2-2) AT5G65165(SDH2-3) AT5G66760(SDH1-1)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
GMX: 
MTR: 
CAM: 
FVE: 
CSV: 
RCU: 
POP: 
POPTR_0001s36050g(POPTRDRAFT_815545) POPTR_0007s12750g(POPTRDRAFT_219180) POPTR_593943
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os07t0134800-01(Os07g0134800) Os08t0120000-01(Os08g0120000) Os09t0370300-01(Os09g0370300)
BDI: 
SBI: 
SORBI_01g006490(SORBIDRAFT_01g006490) SORBI_02g023310(SORBIDRAFT_02g023310)
ZMA: 
100216648(csu474(rpS14)) 100279930(TIDP3457) 100280324 100502233
SITA: 
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
OTA: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YJL045W YKL148C(SDH1) YLL041C(SDH2)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0C05870(NCAS0C05870) NCAS_0F02320(NCAS0F02320)
NDI: 
NDAI_0C03810(NDAI0C03810) NDAI_0H00250(NDAI0H00250)
TPF: 
TPHA_0E02930(TPHA0E02930) TPHA_0F00210(TPHA0F00210)
TBL: 
TBLA_0A10080(TBLA0A10080) TBLA_0E01400(TBLA0E01400)
TDL: 
TDEL_0E03730(TDEL0E03730) TDEL_0G01780(TDEL0G01780)
KAF: 
KAFR_0H03590(KAFR0H03590) KAFR_0L00230(KAFR0L00230)
DHA: 
PIC: 
PGU: 
LEL: 
CAL: 
CTP: 
CDU: 
COT: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
MGR: 
FGR: 
NHE: 
VAL: 
SSL: 
BFU: 
ANI: 
NFI: 
AFM: 
AOR: 
AOR_1_730084(AO090020000415) AOR_1_838024(AO090010000505)
ANG: 
ANI_1_1750024(An02g12770) ANI_1_2706024(An02g07600)
AFV: 
ACT: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
ZTR: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
LBC: 
MPR: 
CCI: 
SCM: 
UMA: 
MGL: 
PGR: 
MBR: 
DDI: 
DPP: 
DFA: 
DFA_01593(sdhA)
ACAN: 
PFA: 
PFD: 
PFH: 
PYO: 
PCB: 
PBE: 
PKN: 
PVX: 
PCY: 
TAN: 
TPV: 
BBO: 
BBOV_IV005280(23.m06368) BBOV_IV007210(23.m06369)
BEQ: 
TGO: 
TET: 
PTM: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
TBR: 
Tb927.8.6580(Tb08.30K1.380)
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:2644269]
  Authors
Kita K, Vibat CR, Meinhardt S, Guest JR, Gennis RB
  Title
One-step purification from Escherichia coli of complex II (succinate: ubiquinone  oxidoreductase) associated with succinate-reducible cytochrome b556.
  Journal
J. Biol. Chem. 264 (1989) 2672-7.
Reference
2
  Authors
Hatefi, Y., Ragan, C.I. and Galante, Y.M.
  Title
The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system.
  Journal
In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd ed., vol. 4, Plenum Press, New York, 1985, p. 1-70.
Reference
3  [PMID:1935955]
  Authors
Moll R, Schafer G
  Title
Purification and characterisation of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile Sulfolobus acidocaldarius.
  Journal
Eur. J. Biochem. 201 (1991) 593-600.
Reference
4  [PMID:12374303]
  Authors
Figueroa P, Leon G, Elorza A, Holuigue L, Araya A, Jordana X
  Title
The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in Arabidopsis thaliana.
  Journal
Plant. Mol. Biol. 50 (2002) 725-34.
Reference
5  [PMID:14527321]
  Authors
Cecchini G
  Title
Function and structure of complex II of the respiratory chain.
  Journal
Annu. Rev. Biochem. 72 (2003) 77-109.
Reference
6  [PMID:14672929]
  Authors
Oyedotun KS, Lemire BD
  Title
The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies.
  Journal
J. Biol. Chem. 279 (2004) 9424-31.
Reference
7  [PMID:15883782]
  Authors
Kurokawa T, Sakamoto J
  Title
Purification and characterization of succinate:menaquinone oxidoreductase from Corynebacterium glutamicum.
  Journal
Arch. Microbiol. 183 (2005) 317-24.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9028-11-9

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