ID A0A0M8ZPV7_9HYME Unreviewed; 277 AA. AC A0A0M8ZPV7; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 25-OCT-2017, entry version 11. 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 ORFNames=WN51_04166 {ECO:0000313|EMBL:KOX68680.1}; OS Melipona quadrifasciata. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; 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 CC dehydrogenase (SDH) that is involved in complex II of the CC mitochondrial electron transport chain and is responsible for CC transferring electrons from succinate to ubiquinone (coenzyme Q). CC {ECO:0000256|RuleBase:RU361237}. CC -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol. CC {ECO:0000256|RuleBase:RU361237}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; 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; CC fumarate from succinate (eukaryal route): step 1/1. CC {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 CC reductase iron-sulfur protein family. 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 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 carrier activity; IEA:InterPro. 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 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. 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; SSF46548; SSF46548; 1. DR SUPFAM; SSF54292; SSF54292; 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|RuleBase:RU361237}; KW 3Fe-4S {ECO:0000256|RuleBase:RU361237}; KW 4Fe-4S {ECO:0000256|RuleBase:RU361237}; KW Complete proteome {ECO:0000313|Proteomes:UP000053105}; KW Iron {ECO:0000256|RuleBase:RU361237}; KW Iron-sulfur {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 Reference proteome {ECO:0000313|Proteomes:UP000053105}; KW Ubiquinone {ECO:0000313|EMBL:KOX68680.1}. FT DOMAIN 46 125 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 168 198 4Fe-4S ferredoxin-type. FT {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 //