ID A0A7S2R1U3_9STRA Unreviewed; 264 AA. AC A0A7S2R1U3; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 6. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000256|RuleBase:RU361237}; DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237}; DE Flags: Fragment; GN ORFNames=EANT1437_LOCUS1900 {ECO:0000313|EMBL:CAD9658098.1}; OS Eucampia antarctica. OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae; OC Biddulphiophycidae; Hemiaulales; Hemiaulaceae; Eucampia. OX NCBI_TaxID=49252 {ECO:0000313|EMBL:CAD9658098.1}; RN [1] {ECO:0000313|EMBL:CAD9658098.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1452 {ECO:0000313|EMBL:CAD9658098.1}; RA Corre E., Pelletier E., Niang G., Scheremetjew M., Finn R., Kale V., RA Holt S., Cochrane G., Meng A., Brown T., Cohen L.; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU361237}; Peripheral membrane protein CC {ECO:0000256|RuleBase:RU361237}; Matrix side CC {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; HBHI01003779; CAD9658098.1; -; Transcribed_RNA. DR AlphaFoldDB; A0A7S2R1U3; -. DR UniPathway; UPA00223; UER01006. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd00207; fer2; 1. DR Gene3D; 1.10.1060.10; -; 1. DR Gene3D; 3.10.20.30; -; 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 Pfam; PF13085; Fer2_3; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR TIGRFAMs; TIGR00384; dhsB; 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 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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 92..176 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 219..249 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAD9658098.1" FT NON_TER 264 FT /evidence="ECO:0000313|EMBL:CAD9658098.1" SQ SEQUENCE 264 AA; 30280 MW; 1D166DF172F6E8A0 CRC64; PPKEFCGLQT KKHRKDRLII TLLNKQYKMF LSSSTQHLSR ALSSTSVQRA FHNSCKRTMS TESLKVSDPV PVQKTERVKY FKIYRWDPEQ KQKPYLSTYP VDLSDCGPMV LDALIKIKNE QDPTLTFRRS CREGICGSCA MNIDGANTLA CLCYIEPMGA GDTSGKATKV YPLPHMYVIK DLVPDMGNFY EQYRSIEPWL QTKKGKKEGQ AEFLQTREDR AKLDGMYECI LCACCSTSCP SYWWNADKYL GPAVLMQAFR WIED //