ID T1JTX0_TETUR Unreviewed; 299 AA.
AC T1JTX0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Name=107366097 {ECO:0000313|EnsemblMetazoa:tetur01g15710.1};
GN Synonyms=SdhB {ECO:0000313|EMBL:BBP41344.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur01g15710.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur01g15710.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
RN [3] {ECO:0000313|EMBL:BBP41344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tsukuba_S {ECO:0000313|EMBL:BBP41344.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:BBP41344.1};
RA Sugimoto N., Takahashi A., Ihara R., Itoh Y., Jouraku A., Van-Leeuwen T.,
RA Osakabe M.;
RT "QTL mapping of high-level resistance against three mitochondrial complex
RT II inhibitors using microsatellite linkage maps in the two-spotted spider
RT mite Tetranychus urticae.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QRG98985.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JPR-R2 complex II {ECO:0000313|EMBL:QRG98985.1};
RA Fotoukkiaii S.M., Mermans C., Wybouw N., Van Leeuwen T.;
RT "Resistance risk assessment of the novel complex II inhibitor pyflubumide
RT in the polyphagous pest Tetranychus urticae.";
RL J. Pest Sci. 9:1085-1096(2020).
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}.
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DR EMBL; CAEY01000486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LC511606; BBP41344.1; -; Genomic_DNA.
DR EMBL; MN820830; QRG98985.1; -; mRNA.
DR RefSeq; XP_015789155.1; XM_015933669.1.
DR AlphaFoldDB; T1JTX0; -.
DR SMR; T1JTX0; -.
DR STRING; 32264.T1JTX0; -.
DR EnsemblMetazoa; tetur01g15710.1; tetur01g15710.1; tetur01g15710.
DR GeneID; 107366097; -.
DR KEGG; tut:107366097; -.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_2_1; -.
DR OMA; DKQMFQS; -.
DR OrthoDB; 119960at2759; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000015104; 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: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 CDD; cd00207; fer2; 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; 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 2: Evidence at transcript level;
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:UP000015104};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 66..147
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 190..220
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 299 AA; 33811 MW; E24415BCD3E024F2 CRC64;
MNSVINLFTK NGKLLSLAST SHLPSVRITS TSNNQAAAAA AAAATSEVPE KRIKKFMVYR
WNPETPEVKP YMQTYEVDLN TCGPMVLDAL IKIKNELDPT LTFRRSCREG ICGSCAMNIG
GGNTLACISR IDTSVEKPMK IYPLPHMYVV KDLVPDMNHF YEQYRSIQPW LQKKDETGFG
KKQNLQSVDD RKKLDGLYEC ILCACCSTSC PSYWWNSDRY LGPAVLMQAY RWVIDSRDES
TEKRLDQLRD PFSLYRCHTI MNCSRTCPKN LNPGRAIGEL KKLLAGWSKK SEPQISGQV
//
