ID A0A061DFR8_THECC Unreviewed; 631 AA.
AC A0A061DFR8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN ORFNames=TCM_000401 {ECO:0000313|EMBL:EOX91114.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX91114.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX91114.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU362051}.
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|RuleBase:RU362051};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362051};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000256|RuleBase:RU362051}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU362051}; Matrix side
CC {ECO:0000256|RuleBase:RU362051}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC ECO:0000256|RuleBase:RU362051}.
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DR EMBL; CM001879; EOX91114.1; -; Genomic_DNA.
DR RefSeq; XP_007046957.1; XM_007046895.2.
DR AlphaFoldDB; A0A061DFR8; -.
DR SMR; A0A061DFR8; -.
DR STRING; 3641.A0A061DFR8; -.
DR EnsemblPlants; EOX91114; EOX91114; TCM_000401.
DR EnsemblPlants; Tc01v2_t003170.1; Tc01v2_p003170.1; Tc01v2_g003170.
DR GeneID; 18610944; -.
DR Gramene; EOX91114; EOX91114; TCM_000401.
DR Gramene; Tc01v2_t003170.1; Tc01v2_p003170.1; Tc01v2_g003170.
DR KEGG; tcc:18610944; -.
DR eggNOG; KOG2403; Eukaryota.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; A0A061DFR8; -.
DR OMA; FHPTGIW; -.
DR OrthoDB; 551958at2759; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000026915; Chromosome 1.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01816; sdhA_forward; 1.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU362051};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR611281-4};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362051};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362051};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transit peptide {ECO:0000256|RuleBase:RU362051};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 48..444
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 499..631
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT MOD_RES 84
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 631 AA; 69809 MW; 0590524BCEE36AC7 CRC64;
MWRCVSRSLR VPYSKRSVSY DSLRSHISKF LDNESVRSPY TIVDHTYDAV VVGAGGAGLR
AAIGLSEHGF NTACITKLFP TRSHTVAAQG GINAALGNMT EDDWRWHMYD TVKGSDWLGD
QDAIQYMCRE APKAVIELEN YGLPFSRTED GKIYQRAFGG QSLDFGKGGQ AYRCACAADR
TGHALLHSLY GQAMKHNTQF FVEYFALDLL MNSDGSCQGV IALNMEDGTL HRFRAVSTIL
ATGGYGRAYF SATSAHTCTG DGNAMVARAG LPLQDLEFVQ FHPTGIYGAG CLITEGSRGE
GGILRNSEGE RFMERYAPTA KDLASRDVVS RSMTMEIREG RGVGPLKDHI YLHLNHLPPE
VLKERLPGIS ETAAIFAGVD VTKEPIPVLP TVHYNMGGIP TNHHGEVVTV RGSNPDSVVP
GLMAAGEAAC ASVHGANRLG ANSLLDIVVF GRACANRVAE IHRPGEKLKP LEKDASEKTI
AWLDKIRNSN GSLPTSKIRL NMQRVMQNNA AVFRTQETLE EGCQLIDEAW ESFHDVKLKD
RSLIWNSDLI ETIELENLLI NACITMHSAE ARKESRGAHA REDFTKRDDE NWMKHTLGYW
ENEKVRLDYR PVHMNTLDDE IESFPPKARV Y
//
