ID   Q00WK0_OSTTA            Unreviewed;       681 AA.
AC   Q00WK0;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=OT_ostta14g00080 {ECO:0000313|EMBL:CAL56758.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CAL56758.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAL56758.1}.
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DR   EMBL; CAID01000014; CAL56758.1; -; Genomic_DNA.
DR   RefSeq; XP_003082803.1; XM_003082755.1.
DR   AlphaFoldDB; Q00WK0; -.
DR   STRING; 70448.Q00WK0; -.
DR   GeneID; 9837612; -.
DR   KEGG; ota:OT_ostta14g00080; -.
DR   InParanoid; Q00WK0; -.
DR   OMA; FHPTGIW; -.
DR   OrthoDB; 551958at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000009170; Chromosome 14.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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:UP000009170};
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          99..494
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          549..681
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          56..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         135
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   681 AA;  73278 MW;  AA95B7DFE41C7CCA CRC64;
     MFASTSRRAL RRGCVGPVAA LATGASAAST AAVSTASMAS ASSMASASAR ASVDARGGRS
     WTNGARGGGR SRRSRDGFAR AYSGTSASSA YEIIDHEYDA LVVGAGGAGL RAAIGLGEHG
     FKTACVTKLF PTRSHTVAAQ GGINAALGNM TEDDWRWHAY DTVKGADWLG DQDAIQYMCR
     EAPKAVIELE KYGMPFSRTD DGRIYQRAFG GQSLDFGKGG QAYRCAAAAD RTGHAMLHTL
     YGAALKHDVQ FFVEYFALDL IMDKGECVGV MALCLEDGTL HRFRSHQTIL ATGGYGRAYF
     SATSAHTCTG DGNAMVARAG LPLQDQEFVQ FHPTGIYGAG CLITEGSRGE GGILRNSEGE
     RFMERYAPSA KDLASRDVVS RAMTMEIREG RGVGKEKDHI YLHLNHLPPE LLAERLPGIS
     ETAAIFAGVD VTKEPIPVIP TVHYNMGGIP TNYKGEVVAP KNGDMDAIVP GLMAAGEAAC
     ASVHGANRLG ANSLLDIVVF GRACANTVSE KLKPGTPHRQ IAADAGSNAV ERLDKIRNSK
     GSAPTAMLRR TMQKVMQDDA AVFRTQESLA NGCKRIDDVA AQLDNLKLTD RSLVWNTDLV
     EALELHNLMP NAQTTMHSAE QRKESRGAHA REDFPDRLDD TWMKHTLAYV ENGKVKIDYR
     PNHHYTLDDE MEVIPPKARV Y
//