ID A0A0L8FTG4_OCTBM Unreviewed; 290 AA. AC A0A0L8FTG4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 12-OCT-2022, entry version 27. 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=OCBIM_22008560mg {ECO:0000313|EMBL:KOF67933.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda; OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF67933.1, ECO:0000313|Proteomes:UP000053454}; RN [1] {ECO:0000313|Proteomes:UP000053454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Albertin C.B., Simakov O., Mitros T., Wang Z.Y., Pungot J.R., RA Edsinger-Gonzalez E., Brenner S., Ragsdale C.W., Rokhsar D.S.; RT "WGS assembly of Octopus bimaculoides."; 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; EC=1.3.5.1; CC Evidence={ECO:0000256|ARBA:ARBA00000030}; 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|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 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; KQ426701; KOF67933.1; -; Genomic_DNA. DR EnsemblMetazoa; Ocbimv22008561m; Ocbimv22008561m.p; Ocbimv22008560m.g. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000053454; 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 (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 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_sf. 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; 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|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU361237}; KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU361237}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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 Neurotoxin {ECO:0000256|ARBA:ARBA00022699}; KW Reference proteome {ECO:0000313|Proteomes:UP000053454}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Toxin {ECO:0000256|ARBA:ARBA00022656}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT DOMAIN 44..137 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 182..212 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" SQ SEQUENCE 290 AA; 32795 MW; 175E52BB20638C6B CRC64; MMAVPCSSLS RLLPISKALV PVLQVMRCAQ TAAAVAAEPS KHVKTFTIYR WDPDKQGDKP RMQSYEIDLN RCGPMVLDAL IKIKNEDDPT LTFRRSCREG ICGSCAMNIG GVNTLACICK IDGNLSKPTK IYPLPHMYVI KDLVPDMNNF YAQYASIEPY LKKKDIKEED IGKEQYLQSV RDRAKLDGLY ECILCACCST SCPSYWWNSD KYLGPAVLMQ AYRWMIDSRD DFTVERLSKM EDKFSVYRCH TIMNCTKTCP KHLNPGLAIG EIKKMLALYK KNAETSAAHA //