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Database: UniProt/TrEMBL
Entry: D2KQI9_SOLLC
LinkDB: D2KQI9_SOLLC
Original site: D2KQI9_SOLLC 
ID   D2KQI9_SOLLC            Unreviewed;       274 AA.
AC   D2KQI9;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 88.
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=100736507 {ECO:0000313|EnsemblPlants:Solyc02g093680.3.1};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EMBL:ACZ71182.1};
RN   [1] {ECO:0000313|EMBL:ACZ71182.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Araujo W.L., Nunes-Nesi A., Osorio S., Usadel B., Fuentes D., Balbo I.,
RA   Lehmann M., Studart-Witkowski C., Jordana X., DaMatta F.M., Fernie A.R.;
RT   "The antisense inhibition of the iron-sulfur subunit of succinate
RT   dehydrogenase in tomato plants.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:Solyc02g093680.3.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc02g093680.3.1};
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [3] {ECO:0000313|EnsemblPlants:Solyc02g093680.3.1}
RP   IDENTIFICATION.
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc02g093680.3.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2019) to UniProtKB.
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}.
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DR   EMBL; GU262989; ACZ71182.1; -; mRNA.
DR   RefSeq; NP_001234860.1; NM_001247931.3.
DR   AlphaFoldDB; D2KQI9; -.
DR   SMR; D2KQI9; -.
DR   STRING; 4081.D2KQI9; -.
DR   PaxDb; 4081-Solyc02g093680-2-1; -.
DR   EnsemblPlants; Solyc02g093680.3.1; Solyc02g093680.3.1; Solyc02g093680.3.
DR   GeneID; 100736507; -.
DR   Gramene; Solyc02g093680.3.1; Solyc02g093680.3.1; Solyc02g093680.3.
DR   KEGG; sly:100736507; -.
DR   eggNOG; KOG3049; Eukaryota.
DR   HOGENOM; CLU_044838_0_1_1; -.
DR   InParanoid; D2KQI9; -.
DR   OrthoDB; 119960at2759; -.
DR   BRENDA; 1.3.5.1; 3101.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000004994; Chromosome 2.
DR   ExpressionAtlas; D2KQI9; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045273; C:respiratory chain complex II; IEA:UniProt.
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:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0006124; P:ferredoxin metabolic process; IEA:UniProt.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
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   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   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
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|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU361237};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU361237};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          46..134
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          177..207
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   274 AA;  30862 MW;  89685B5DFB6F77FC CRC64;
     MATSLIRRAI SRVQSSAPAA RLLVARAHAS DSQAQKVESK PNLKSFQIYR WTPDNPGKPE
     LKEYKIDLKE CGPMVLDALI KIKNEIDPTL TFRRSCREGI CGSCAMNIDG CNGLACLTKI
     SSDSESTITP LPHMFVIKDL VVDMTNFYNQ YKSIEPWLKR KTPAPTPGKE IPQSKSDRAK
     LDGMYECILC ACCSTSCPSY WWNPESYLGP AALLHANRWI MDSRDEYTQE RLDAVNDEFK
     LYRCHTILNC SRACPKGLNP GKHIQNIKKL EMAP
//
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