ID   SDHA_ORYSJ              Reviewed;         630 AA.
AC   Q6ZDY8; A0A0P0X2R9; Q0D8R4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=FP;
DE   Flags: Precursor;
GN   Name=SDH1; OrderedLocusNames=Os07g0134800, LOC_Os07g04240;
GN   ORFNames=P0507H12.27;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=19924544; DOI=10.1007/s11103-009-9573-z;
RA   Huang S., Taylor N.L., Narsai R., Eubel H., Whelan J., Millar A.H.;
RT   "Functional and composition differences between mitochondrial complex II in
RT   Arabidopsis and rice are correlated with the complex genetic history of the
RT   enzyme.";
RL   Plant Mol. Biol. 72:331-342(2010).
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:0000250|UniProtKB:P31040}.
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:0000250|UniProtKB:P31040};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (eukaryal route): step 1/1.
CC       {ECO:0000250|UniProtKB:P31040}.
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:0000269|PubMed:19924544}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:O82663}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O82663}; Matrix side
CC       {ECO:0000250|UniProtKB:O82663}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; AP004338; BAC83515.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF20759.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAS99963.1; -; Genomic_DNA.
DR   EMBL; AK065901; BAG89728.1; -; mRNA.
DR   RefSeq; XP_015646992.1; XM_015791506.1.
DR   AlphaFoldDB; Q6ZDY8; -.
DR   SMR; Q6ZDY8; -.
DR   STRING; 39947.Q6ZDY8; -.
DR   PaxDb; 39947-Q6ZDY8; -.
DR   EnsemblPlants; Os07t0134800-01; Os07t0134800-01; Os07g0134800.
DR   GeneID; 4342350; -.
DR   Gramene; Os07t0134800-01; Os07t0134800-01; Os07g0134800.
DR   KEGG; osa:4342350; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   HOGENOM; CLU_014312_6_1_1; -.
DR   InParanoid; Q6ZDY8; -.
DR   OMA; FHPTGIW; -.
DR   OrthoDB; 551958at2759; -.
DR   PlantReactome; R-OSA-1119533; TCA cycle (plant).
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   ExpressionAtlas; Q6ZDY8; baseline and differential.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR   GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
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.
DR   Genevisible; Q6ZDY8; OS.
PE   1: Evidence at protein level;
KW   Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..630
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000247593"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         52..57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         75..90
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         260
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         426
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         437
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         442..443
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   MOD_RES         83
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ   SEQUENCE   630 AA;  68854 MW;  9BDEE1ABC77CF08C CRC64;
     MWRGCVSRGL RSLSKGKGSS SSAPVSAAAR LFSTASSSYT VVDHSYDAVV VGAGGAGLRA
     AIGLSEHGFN TACITKLFPT RSHTVAAQGG INAALGNMTE DDWRWHMYDT VKGSDWLGDQ
     DSIQYMCREA PKAVIELENY GLPFSRTEDG KIYQRAFGGQ SLDFGKGGQA YRCACAADRT
     GHAMLHTLYG QAMKHNTQFF VEYFALDLIM DSEGTCQGVI ALNMEDGTLH RFRATNTILA
     TGGYGRAYFS ATSAHTCTGD GNAMVARAGL PLQDLEFVQF HPTGIYGAGC LITEGSRGEG
     GILRNSEGER FMERYAPTAK DLASRDVVSR SMTMEIREGR GVGPLKDHIY LHLNHLPPEV
     LKERLPGISE TAAIFAGVDV TKEPIPVLPT VHYNMGGIPT NYHGEVVTMK GDNPDSVVPG
     LMAAGEAACA SVHGANRLGA NSLLDIVVFG RACANRVAET AKPGEKQKPL QKSAGEKTIA
     WLDKLRNANG SLPTSKIRLN MQRVMQNNAA VFRTQETLEE GCKLITKAWE SYHDVKISDR
     SLIWNSDLIE TIELENLLIN ACITMHSAEA RKESRGAHAR EDFTKRDDEQ WMKHSLGYWE
     NEKVRLAYRP VHMNTLDSEV ESFPPKARVY
//