ID SDHB_MYCMD Reviewed; 295 AA. AC P32420; A0A0D1CWY8; Q12722; Q4PGB9; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 162. 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=CBXR; ORFNames=UMAG_00844; OS Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Ustilaginomycetes; Ustilaginales; Ustilaginales incertae sedis; OC Mycosarcoma. OX NCBI_TaxID=5270; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 38509 / 92; RX PubMed=1879000; DOI=10.1007/bf00312739; RA Keon J.P.R., White G.A., Hargreaves J.A.; RT "Isolation, characterization and sequence of a gene conferring resistance RT to the systemic fungicide carboxin from the maize smut pathogen, Ustilago RT maydis."; RL Curr. Genet. 19:475-481(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1423716; DOI=10.1007/bf00351470; RA Broomfield P.L.E., Hargreaves J.A.; RT "A single amino-acid change in the iron-sulphur protein subunit of RT succinate dehydrogenase confers resistance to carboxin in Ustilago RT maydis."; RL Curr. Genet. 22:117-121(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14603 / FGSC 9021 / UM521; RX PubMed=17080091; DOI=10.1038/nature05248; RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W., RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., RA Birren B.W.; RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago RT maydis."; RL Nature 444:97-101(2006). RN [4] RP GENOME REANNOTATION. RC STRAIN=DSM 14603 / FGSC 9021 / UM521; RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.; RL Submitted (SEP-2014) 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 = 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 -!- 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; X62762; CAA44612.1; -; Genomic_DNA. DR EMBL; Z11738; CAA77798.1; -; Genomic_DNA. DR EMBL; CM003141; KIS70918.1; -; Genomic_DNA. DR PIR; S26978; S26978. DR RefSeq; XP_011386878.1; XM_011388576.1. DR AlphaFoldDB; P32420; -. DR SMR; P32420; -. DR FunCoup; P32420; 296. DR STRING; 237631.P32420; -. DR EnsemblFungi; KIS70918; KIS70918; UMAG_00844. DR GeneID; 23562034; -. DR KEGG; uma:UMAG_00844; -. DR VEuPathDB; FungiDB:UMAG_00844; -. DR eggNOG; KOG3049; Eukaryota. DR HOGENOM; CLU_044838_0_2_1; -. DR InParanoid; P32420; -. DR OMA; DGQYFGP; -. DR OrthoDB; 1696654at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000000561; Chromosome 2. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central. 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:0009060; P:aerobic respiration; IBA:GO_Central. DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd00207; fer2; 1. 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; PRK05950.1; 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 Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..295 FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur FT subunit, mitochondrial" FT /id="PRO_0000010352" FT DOMAIN 67..144 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 185..215 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 106 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 126 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 195 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 201 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 205 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250" FT BINDING 210 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /ligand_note="ligand shared with DHSD" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250" FT BINDING 262 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT VARIANT 253 FT /note="H -> L (in carboxin-resistant mutant)" SQ SEQUENCE 295 AA; 33282 MW; F374A20BA8F8E7E5 CRC64; MSLFNVSNGL RTALRPSVAS SSRVAAFSTT AAARLATPTS DNVGSSGKPQ HLKQFKIYRW NPDKPSEKPR LQSYTLDLNQ TGPMVLDALI KIKNEIDPTL TFRRSCREGI CGSCAMNIDG VNTLACLCRI DKQNDTKIYP LPHMYIVKDL VPDLTQFYKQ YRSIEPFLKS NNTPSEGEHL QSPEERRRLD GLYECILCAC CSTSCPSYWW NQDEYLGPAV LMQAYRWMAD SRDDFGEERR QKLENTFSLY RCHTIMNCSR TCPKNLNPGK AIAQIKKDMA VGAPKASERP IMASS //