ID A0A0M8ZPV7_9HYME Unreviewed; 277 AA. AC A0A0M8ZPV7; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 02-OCT-2024, entry version 35. 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 ORFNames=WN51_04166 {ECO:0000313|EMBL:KOX68680.1}; OS Melipona quadrifasciata. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; OC Anthophila; Apidae; Melipona. OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX68680.1, ECO:0000313|Proteomes:UP000053105}; RN [1] {ECO:0000313|EMBL:KOX68680.1, ECO:0000313|Proteomes:UP000053105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX68680.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KOX68680.1}; RA Pan H., Kapheim K.; RT "The genome of Melipona quadrifasciata."; RL Submitted (JUL-2015) 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; 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 -!- 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; KQ435922; KOX68680.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0M8ZPV7; -. DR STRING; 166423.A0A0M8ZPV7; -. DR OrthoDB; 119960at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000053105; Unassembled WGS sequence. 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: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 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 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|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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000053105}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}; KW Ubiquinone {ECO:0000313|EMBL:KOX68680.1}. FT DOMAIN 46..125 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 168..198 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" SQ SEQUENCE 277 AA; 31527 MW; 5A516FD2DA70E1E7 CRC64; MAGITPQVCR NAFRQVRKFH ISSNQNAEAR LKTFAVYRWN PDKPDEKPYL QEYKVDLSTC GPMVLDALIK IKNEIDPTLT FRRSCREGIC GSCAMNIGGT NTLACISKID TNTSTTSKIY PLPHMYIVKD LVPDLNNFYN QYRSIQPWLQ RGDGQKAGSK QYLQSVEDRK KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW IIDSRDNKTK ERLEKLRDPY SVYRCHTIMN CTRTCPKGLN PGKAIAEIKK LLANISEKQK PGLDAAV //