ID F9XG45_ZYMTI Unreviewed; 297 AA. AC F9XG45; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 04-NOV-2026, entry version 76. 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 Name=SDH2 {ECO:0000313|EMBL:EGP85729.1}; GN ORFNames=MYCGRDRAFT_74146 {ECO:0000313|EMBL:EGP85729.1}; OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch OS fungus) (Septoria tritici). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria. OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP85729.1, ECO:0000313|Proteomes:UP000008062}; RN [1] {ECO:0000313|EMBL:EGP85729.1, ECO:0000313|Proteomes:UP000008062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062}; RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070; RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F., RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A., RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A., RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J., RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B., RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B., RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A., RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R., RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J., RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H., RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H., RA Oliver R.P., Grigoriev I.V., Kema G.H.J.; RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola RT reveals dispensome structure, chromosome plasticity, and stealth RT pathogenesis."; RL PLoS Genet. 7:E1002070-E1002070(2011). 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 = fumarate + a quinol; 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:ARBA00049220}; 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; CM001202; EGP85729.1; -; Genomic_DNA. DR RefSeq; XP_003850753.1; XM_003850705.1. DR AlphaFoldDB; F9XG45; -. DR SMR; F9XG45; -. DR FunCoup; F9XG45; 694. DR STRING; 336722.F9XG45; -. DR GeneID; 13397827; -. DR KEGG; ztr:MYCGRDRAFT_74146; -. DR VEuPathDB; FungiDB:ZTRI_7.463; -. DR eggNOG; KOG3049; Eukaryota. DR HOGENOM; CLU_044838_0_0_1; -. DR InParanoid; F9XG45; -. DR OrthoDB; 1696654at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000008062; Chromosome 7. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0008177; F:succinate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:TreeGrafter. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR FunFam; 3.10.20.30:FF:000007; Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; 1. DR FunFam; 1.10.1060.10:FF:000001; Succinate dehydrogenase iron-sulfur subunit SdhB; 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; IPR050573; SDH/FRD_Iron-Sulfur. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR NCBIfam; TIGR00384; dhsB; 1. DR NCBIfam; NF004616; sdhB; 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|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361237}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Iron {ECO:0000256|ARBA:ARBA00023004, 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|ARBA:ARBA00022723, KW 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 ECO:0000313|EMBL:EGP85729.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008062}; KW Transport {ECO:0000256|ARBA:ARBA00022448}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 78..157 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 199..229 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT REGION 33..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 297 AA; 33667 MW; A50010A24F48F6D4 CRC64; MALRLATRRF APIAFRRGMA TTIEHTKEPI SATAEALSAS RPPIKETKTS TVKEPQMDAD AKTKTFHIYR WNPDQPTDKP RMQSYTLDLN KTGPMMLDAL IRIKNEVDPT LTFRRSCREG ICGSCAMNID GVNTLACLCR IPTDTAKETR IYPLPHTYVV KDLVPDMTQF YKQYKSIKPY LQRDTAPPDG KENRQSVADR KKLDGLYECI LCACCSTSCP SYWWNSEEYL GPAVLLQSYR WINDSRDEKT AQRKDALNNS MSLYRCHTIL NCSRTCPKGL NPALAIAEIK KSMAFTG //