ID C5M396_CANTT Unreviewed; 263 AA. AC C5M396; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 24-JAN-2024, entry version 70. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000256|ARBA:ARBA00016766, ECO:0000256|RuleBase:RU361237}; DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU361237}; GN ORFNames=CTRG_00535 {ECO:0000313|EMBL:EER35796.1}; OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER35796.1, ECO:0000313|Proteomes:UP000002037}; RN [1] {ECO:0000313|EMBL:EER35796.1, ECO:0000313|Proteomes:UP000002037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037}; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M., RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R., RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., RA Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase CC (SDH) that is involved in complex II of the mitochondrial electron CC transport chain and is responsible for transferring electrons from CC succinate to ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU361237}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + succinate = a quinol + fumarate; CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; CC Evidence={ECO:0000256|ARBA:ARBA00000030}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|RuleBase:RU361237}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000256|RuleBase:RU361237}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|RuleBase:RU361237}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate CC from succinate (eukaryal route): step 1/1. CC {ECO:0000256|ARBA:ARBA00004788, ECO:0000256|RuleBase:RU361237}. CC -!- SUBUNIT: Component of complex II composed of four subunits: a CC flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b CC composed of a large and a small subunit. CC {ECO:0000256|ARBA:ARBA00011421}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443, CC ECO:0000256|RuleBase:RU361237}; Matrix side CC {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433, CC ECO:0000256|RuleBase:RU361237}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG692395; EER35796.1; -; Genomic_DNA. DR RefSeq; XP_002545754.1; XM_002545708.1. DR AlphaFoldDB; C5M396; -. DR STRING; 294747.C5M396; -. DR EnsemblFungi; CTRG_00535-t43_1; CTRG_00535-t43_1-p1; CTRG_00535. DR GeneID; 8296854; -. DR KEGG; ctp:CTRG_00535; -. DR VEuPathDB; FungiDB:CTRG_00535; -. DR eggNOG; KOG3049; Eukaryota. DR HOGENOM; CLU_044838_0_2_1; -. DR OrthoDB; 119960at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000002037; Unassembled WGS sequence. DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IEA:EnsemblFungi. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IEA:EnsemblFungi. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:EnsemblFungi. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd00207; fer2; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR NCBIfam; TIGR00384; dhsB; 1. DR PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1. DR Pfam; PF13085; Fer2_3; 1. DR Pfam; PF13534; Fer4_17; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU361237}; KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU361237}; KW 4Fe-4S {ECO:0000256|RuleBase:RU361237}; KW Iron {ECO:0000256|RuleBase:RU361237}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237}; KW Membrane {ECO:0000256|RuleBase:RU361237}; KW Metal-binding {ECO:0000256|RuleBase:RU361237}; KW Mitochondrion {ECO:0000256|RuleBase:RU361237}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU361237}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000002037}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 43..124 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 166..196 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" SQ SEQUENCE 263 AA; 30140 MW; D9AEDAE990CBA00A CRC64; MFRSVLRQQK AAQFSIRSLA TATTEKAPRL KKFQVYRWNP DTPEVQPKMQ TYEVDLNKCG PMVLDALLKI KNEQDATLTL RRSCREGICG SCAMNIGGRN TLACLCRIDQ DETKDLKVYP LPHMFVVRDL VPDLTHFYKQ YKSIEPYLQR DSNPADGREN LQSIEDRAKL DGLYECILCA CCSTSCPSYW WNQQQYLGPA VLMQAYRWLI DSRDQATASR KAMLQNSMSL YRCHTIMNCT KTCPKGLNPG RAIAEVKKQL AFD //