ID SDHB_UROFA Reviewed; 283 AA. AC Q70KF8; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 83. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; DE EC=1.3.5.1; DE AltName: Full=Iron-sulfur subunit of complex II; DE Short=Ip; DE Flags: Precursor; GN Name=SDH2; Synonyms=sucDH1; OS Uromyces fabae (Rust fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces. OX NCBI_TaxID=55588; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wirsel S.G.R., Voegele R.T., Baenninger R., Hahn M., Mendgen K.W.; RT "Prelude to transformation: characterization of the beta-tubulin and RT succinate dehydrogenase genes from the rust fungus Uromyces fabae."; RL Submitted (JUL-2003) 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:0000250}. 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 -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate CC from succinate (eukaryal route): step 1/1. 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. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase CC iron-sulfur protein family. {ECO:0000305}. 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; AJ575686; CAE02642.1; -; Genomic_DNA. DR AlphaFoldDB; Q70KF8; -. DR SMR; Q70KF8; -. 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: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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 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; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Transit peptide; Transport; Tricarboxylic acid cycle. FT TRANSIT 1..? FT /note="Mitochondrion" FT CHAIN ?..283 FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur FT subunit, mitochondrial" FT /id="PRO_0000010351" FT DOMAIN 66..145 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 186..216 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 105 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 110 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 113 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 125 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 196 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 199 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 206 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250" FT BINDING 211 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /ligand_note="ligand shared with DHSD" FT /evidence="ECO:0000250" FT BINDING 253 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250" FT BINDING 259 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" SQ SEQUENCE 283 AA; 32104 MW; 058945BABE06185F CRC64; MINIPNSIRP FIRSANRTPC YLRSISSSSS SSFATPAEEH AGKQPSSAVP VKEFSIYRWN PDEPSKKPTL QTYSIDLKKC GPMVLDALIK IKNELDPTLT FRRSCREGIC GSCAMNIDGV NTLACLKRIN KETSAPVKIY PLPHMYIIKD LVPDMTHFYK QYKSIEPFLK NDNPPAQGEF LQSPEDRKKL DGMYECILCA CCSTSCPSYW WNQDEYLGPA VLMQAYRWMA DSRDSYGEDR KEKLQNTLSL YRCHTIFNCT KTCPKGLNPA KAISHIKREM ASA //