ID D7MJ52_ARALL Unreviewed; 280 AA. AC D7MJ52; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000256|RuleBase:RU361237}; DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237}; GN Name=SDH2-2 {ECO:0000313|EMBL:EFH46947.1}; GN ORFNames=ARALYDRAFT_493917 {ECO:0000313|EMBL:EFH46947.1}; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K., RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J., RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y., RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size RT change."; RL Nat. Genet. 43:476-481(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|ARBA:ARBA00002787, CC 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; CC Evidence={ECO:0000256|RuleBase:RU361237}; 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 eight subunits in plants: CC four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a flavoprotein CC (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a CC large and a small subunit.), as well as four subunits unknown in CC mitochondria from bacteria and heterotrophic eukaryotes. CC {ECO:0000256|ARBA:ARBA00011313}. 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; GL348719; EFH46947.1; -; Genomic_DNA. DR RefSeq; XP_002870688.1; XM_002870642.1. DR AlphaFoldDB; D7MJ52; -. DR STRING; 81972.D7MJ52; -. DR EnsemblPlants; fgenesh2_kg.7__3350__AT5G40650.1; fgenesh2_kg.7__3350__AT5G40650.1; fgenesh2_kg.7__3350__AT5G40650.1. DR GeneID; 9304714; -. DR Gramene; fgenesh2_kg.7__3350__AT5G40650.1; fgenesh2_kg.7__3350__AT5G40650.1; fgenesh2_kg.7__3350__AT5G40650.1. DR KEGG; aly:9304714; -. DR eggNOG; KOG3049; Eukaryota. DR HOGENOM; CLU_044838_0_2_1; -. DR OrthoDB; 119960at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IEA:EnsemblPlants. 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 {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|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361237}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237}; KW Membrane {ECO:0000256|ARBA:ARBA00022792, 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|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU361237}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 51..140 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 183..213 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" SQ SEQUENCE 280 AA; 31247 MW; 1000FC758818AF26 CRC64; MTFGLIGRVV GTKSSRLYTA ARLIPARWTS TGSEAQSKAS TGGGGASLKT FQIYRWNPDN PGKPELQDYQ IDLKDCGPMV LDALIKIKNE MDPSLTFRRS CREGICGSCA MNIDGCNGLA CLTKIESGSK ETTITPLPHM FVIKDLVVDM TNFYNQYKSI EPWLKRKNPA SVPGKEILQS KKDRAKLDGM YECILCACCS TSCPSYWWNP ESYLGPAALL HANRWISDSR DEYTKERLEA IDDEFKLYRC HTILNCARAC PKGLNPGKQI THIKQLQKSG //