ID 1.3.5.1 DE succinate dehydrogenase. AN fumarate reductase (menaquinone). AN succinate dehydrogenase (menaquinone). AN succinate dehydrogenase (quinone). AN succinate dehydrogenase (ubiquinone). AN succinic dehydrogenase. CA a quinone + succinate = a quinol + fumarate. CC -!- A complex generally comprising an FAD-containing component that also CC binds the carboxylate substrate (A subunit), a component that CC contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], CC and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component CC (C, or C and D subunits) that is also the site of the interaction CC with quinones. CC -!- The enzyme is found in the inner mitochondrial membrane in eukaryotes CC and the plasma membrane of bacteria and archaea, with the hydrophilic CC domain extending into the mitochondrial matrix and the cytoplasm, CC respectively. CC -!- Under aerobic conditions the enzyme catalyzes succinate oxidation, CC a key step in the citric acid (TCA) cycle, transferring the electrons CC to quinones in the membrane, thus linking the TCA cycle with the CC aerobic respiratory chain (where it is known as complex II). CC -!- Under anaerobic conditions the enzyme functions as a fumarate CC reductase, transferring electrons from the quinol pool to fumarate, CC and participating in anaerobic respiration with fumarate as the CC terminal electron acceptor. CC -!- The enzyme interacts with the quinone produced by the organism, such CC as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, CC rhodoquinone etc. Some of the enzymes contain two heme subunits in CC their membrane anchor subunit. CC -!- These enzymes catalyze an electrogenic reaction and are thus CC classified as EC 7.1.1.12. CC -!- Formerly EC 1.3.5.4. DR Q9Z4P0, FRD2_SHEFN ; P00363, FRDA_ECOLI ; P44894, FRDA_HAEIN ; DR Q9ZMP0, FRDA_HELPJ ; O06913, FRDA_HELPY ; P64175, FRDA_MYCBO ; DR P9WN90, FRDA_MYCTO ; P9WN91, FRDA_MYCTU ; P20922, FRDA_PROVU ; DR V3TQ67, FRDA_SERS3 ; Q07WU7, FRDA_SHEFN ; P0C278, FRDA_SHEFR ; DR P83223, FRDA_SHEON ; P17412, FRDA_WOLSU ; P0AC49, FRDB_ECO57 ; DR P0AC48, FRDB_ECOL6 ; P0AC47, FRDB_ECOLI ; P44893, FRDB_HAEIN ; DR Q9ZMP1, FRDB_HELPJ ; O06914, FRDB_HELPY ; P9WN88, FRDB_MYCTO ; DR P9WN89, FRDB_MYCTU ; P20921, FRDB_PROVU ; P0AC50, FRDB_SHIFL ; DR P17596, FRDB_WOLSU ; O82663, SDHA1_ARATH; Q33862, SDHA1_ASCSU; DR Q9ZPX5, SDHA2_ARATH; Q8WSR3, SDHA2_ASCSU; Q6PA58, SDHAA_XENLA; DR Q801S2, SDHAB_XENLA; P08065, SDHA_BACSU ; P31039, SDHA_BOVIN ; DR Q09508, SDHA_CAEEL ; Q9YHT1, SDHA_CHICK ; P51054, SDHA_COXBU ; DR Q7ZVF3, SDHA_DANRE ; Q9U3X4, SDHA_DICDI ; Q94523, SDHA_DROME ; DR P0AC43, SDHA_ECO57 ; P0AC42, SDHA_ECOL6 ; P0AC41, SDHA_ECOLI ; DR P31040, SDHA_HUMAN ; Q8HXW3, SDHA_MACFA ; Q0QF17, SDHA_MESAU ; DR Q8K2B3, SDHA_MOUSE ; Q6ZDY8, SDHA_ORYSJ ; Q59661, SDHA_PARDE ; DR Q0QF01, SDHA_PIG ; Q5R616, SDHA_PONAB ; Q920L2, SDHA_RAT ; DR Q1RHB9, SDHA_RICBR ; Q92J97, SDHA_RICCN ; Q4UJM1, SDHA_RICFE ; DR P31038, SDHA_RICPR ; Q68XN9, SDHA_RICTY ; Q8ZQU3, SDHA_SALTY ; DR Q9UTJ7, SDHA_SCHPO ; G4V4G6, SDHA_SERS3 ; Q28ED0, SDHA_XENTR ; DR Q00711, SDHA_YEAST ; Q8LBZ7, SDHB1_ARATH; Q9S827, SDHB1_ORYSJ; DR Q8LB02, SDHB2_ARATH; Q6H4G3, SDHB2_ORYSJ; Q9FJP9, SDHB3_ARATH; DR O44074, SDHB_ASCSU ; P08066, SDHB_BACSU ; Q3T189, SDHB_BOVIN ; DR A8WPF0, SDHB_CAEBR ; Q09545, SDHB_CAEEL ; Q6FWS8, SDHB_CANGA ; DR Q9YHT2, SDHB_CHICK ; P48932, SDHB_CHOCR ; P51053, SDHB_COXBU ; DR P48933, SDHB_CYACA ; A5PL98, SDHB_DANRE ; Q55CC2, SDHB_DICDI ; DR P21914, SDHB_DROME ; P07014, SDHB_ECOLI ; Q75CI4, SDHB_EREGS ; DR P21912, SDHB_HUMAN ; Q9CQA3, SDHB_MOUSE ; Q59662, SDHB_PARDE ; DR Q007T0, SDHB_PIG ; P80477, SDHB_PORPU ; P21913, SDHB_RAT ; DR P80480, SDHB_RECAM ; Q1RGP3, SDHB_RICBR ; Q92JJ8, SDHB_RICCN ; DR Q4UN71, SDHB_RICFE ; Q9ZEA1, SDHB_RICPR ; Q68XS0, SDHB_RICTY ; DR Q8ZQU2, SDHB_SALTY ; P21911, SDHB_SCHPO ; Q70KF8, SDHB_UROFA ; DR P32420, SDHB_USTMA ; Q3B8J8, SDHB_XENLA ; B0BM36, SDHB_XENTR ; DR P21801, SDHB_YEAST ; O42772, SDHB_ZYMTR ; P47052, SDHX_YEAST ; //