ID   SDHA2_ARATH             Reviewed;         632 AA.
AC   Q9ZPX5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit 2 of complex II;
DE            Short=FP;
DE   Flags: Precursor;
GN   Name=SDH1-2; OrderedLocusNames=At2g18450; ORFNames=T30D6.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12374303; DOI=10.1023/a:1019926301981;
RA   Figueroa P., Leon G., Elorza A., Holuigue L., Araya A., Jordana X.;
RT   "The four subunits of mitochondrial respiratory complex II are encoded by
RT   multiple nuclear genes and targeted to mitochondria in Arabidopsis
RT   thaliana.";
RL   Plant Mol. Biol. 50:725-734(2002).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=15604729; DOI=10.1007/s11103-004-2316-2;
RA   Millar A.H., Eubel H., Jansch L., Kruft V., Heazlewood J.L., Braun H.P.;
RT   "Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes
RT   contain plant specific subunits.";
RL   Plant Mol. Biol. 56:77-90(2004).
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:15604729}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14671022}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14671022}; Matrix side
CC       {ECO:0000269|PubMed:14671022}.
CC   -!- TISSUE SPECIFICITY: Expressed at a low level.
CC       {ECO:0000269|PubMed:12374303}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC006439; AAD15493.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06769.1; -; Genomic_DNA.
DR   EMBL; AK119142; BAC43712.1; -; mRNA.
DR   EMBL; BT005938; AAO64873.1; -; mRNA.
DR   PIR; D84564; D84564.
DR   RefSeq; NP_179435.1; NM_127401.3.
DR   AlphaFoldDB; Q9ZPX5; -.
DR   SMR; Q9ZPX5; -.
DR   BioGRID; 1716; 6.
DR   STRING; 3702.Q9ZPX5; -.
DR   PaxDb; 3702-AT2G18450-1; -.
DR   ProteomicsDB; 232968; -.
DR   EnsemblPlants; AT2G18450.1; AT2G18450.1; AT2G18450.
DR   GeneID; 816359; -.
DR   Gramene; AT2G18450.1; AT2G18450.1; AT2G18450.
DR   KEGG; ath:AT2G18450; -.
DR   Araport; AT2G18450; -.
DR   TAIR; AT2G18450; SDH1-2.
DR   eggNOG; KOG2403; Eukaryota.
DR   HOGENOM; CLU_014312_6_1_1; -.
DR   InParanoid; Q9ZPX5; -.
DR   OMA; WEEGNVK; -.
DR   OrthoDB; 551958at2759; -.
DR   PhylomeDB; Q9ZPX5; -.
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:Q9ZPX5; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZPX5; baseline and differential.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
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:0000104; F:succinate dehydrogenase activity; TAS:TAIR.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; TAS:TAIR.
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:SF72; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT 2, 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; Q9ZPX5; AT.
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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..632
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit 2, mitochondrial"
FT                   /id="PRO_0000247592"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         54..59
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         77..92
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         262
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         428
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         439
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         444..445
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   MOD_RES         85
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ   SEQUENCE   632 AA;  69363 MW;  DEC34651679CEF88 CRC64;
     MWRCLRVASS SRRSESNGAF ITSQLSRFFS APPSAGDKSS YTIVDHTYDA VVVGAGGAGL
     RAAIGLSEHG FNTACITKLF PTRSHTVAAQ GGINAALGNM SVDDWRWHMY DTVKGSDWLG
     DQDAIQYMCR EAPKAVIELE NYGLPFSRTE DGKIYQRAFG GQSLEFGIGG QAYRCACAAD
     RTGHALLHTL YGQAMKHNTQ FFVEYFALDL IMNSDGTCQG VIALNMEDGT LHRFHAGSTI
     LATGGYGRAY FSATSAHTCT GDGNAMVARA GLPLQDLEFV QFHPTGIYGA GCLITEGARG
     EGGILRNSEG EKFMDRYAPT ARDLASRDVV SRSMTMEIRQ GRGAGPMKDY LYLYLNHLPP
     EVLKERLPGI SETAAIFAGV DVTREPIPVL PTVHYNMGGI PTNYHGEVIT LRGDDPDAVV
     PGLMAAGEAA CASVHGANRL GANSLLDIVV FGRACANRVA EIQKPGEKLK PLEKDAGEKS
     IEWLDRIRNS NGSLPTSKIR LNMQRVMQNN AAVFRTQETL EEGCDLIDKT WDSFGDVKVT
     DRSMIWNSDL IETMELENLL VNACITMHSA EARKESRGAH AREDFTKRDD ANWMKHTLGY
     WEEGNVKLEY RPVHMKTLDD EVDTFPPKPR VY
//