ID SDHA1_ARATH Reviewed; 634 AA.
AC O82663;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit 1 of complex II;
DE Short=FP;
DE Flags: Precursor;
GN Name=SDH1-1; OrderedLocusNames=At5g66760; ORFNames=MSN2.16;
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 [MRNA].
RC STRAIN=cv. C24;
RA Machuy N., Klein M., Mueller-Roeber B.;
RT "Cloning and characterization of succinyl-CoA-ligase from Arabidopsis
RT thaliana.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [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 PROTEIN SEQUENCE OF 160-170.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.127.4.1694;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [6]
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 [7]
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 [8]
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-32.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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, ECO:0000305|PubMed:25732537}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14671022}; Matrix side
CC {ECO:0000269|PubMed:14671022}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in flowers and
CC inflorescences. {ECO:0000269|PubMed:12374303}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; AJ001809; CAA05025.1; -; mRNA.
DR EMBL; AB018119; BAA97282.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98260.1; -; Genomic_DNA.
DR EMBL; AF367341; AAK32928.1; -; mRNA.
DR EMBL; AY045674; AAK74032.1; -; mRNA.
DR EMBL; AF436833; AAL32015.1; -; mRNA.
DR EMBL; AY124812; AAM70521.1; -; mRNA.
DR PIR; T51815; T51815.
DR RefSeq; NP_201477.1; NM_126074.3.
DR AlphaFoldDB; O82663; -.
DR SMR; O82663; -.
DR BioGRID; 22051; 13.
DR IntAct; O82663; 2.
DR MINT; O82663; -.
DR STRING; 3702.O82663; -.
DR SwissPalm; O82663; -.
DR PaxDb; 3702-AT5G66760-1; -.
DR ProteomicsDB; 232967; -.
DR EnsemblPlants; AT5G66760.1; AT5G66760.1; AT5G66760.
DR GeneID; 836809; -.
DR Gramene; AT5G66760.1; AT5G66760.1; AT5G66760.
DR KEGG; ath:AT5G66760; -.
DR Araport; AT5G66760; -.
DR TAIR; AT5G66760; SDH1-1.
DR eggNOG; KOG2403; Eukaryota.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; O82663; -.
DR OMA; SAIMRAY; -.
DR OrthoDB; 551958at2759; -.
DR PhylomeDB; O82663; -.
DR BioCyc; ARA:AT5G66760-MONOMER; -.
DR BioCyc; MetaCyc:AT5G66760-MONOMER; -.
DR UniPathway; UPA00223; UER01006.
DR PRO; PR:O82663; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82663; baseline and differential.
DR Genevisible; O82663; AT.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
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: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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 33..634
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit 1, mitochondrial"
FT /id="PRO_0000158659"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 56..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 79..94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 430
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 446..447
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MOD_RES 87
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ SEQUENCE 634 AA; 69656 MW; AECE471C7AD43B84 CRC64;
MWRCVSRGFR APASKTSSLF DGVSGSRFSR FFSTGSTDTR SSYTIVDHTY DAVVVGAGGA
GLRAAIGLSE HGFNTACITK LFPTRSHTVA AQGGINAALG NMSEDDWRWH MYDTVKGSDW
LGDQDAIQYM CREAPKAVIE LENYGLPFSR TEEGKIYQRA FGGQSLDFGK GGQAYRCACA
ADRTGHALLH TLYGQAMKHN TQFFVEYFAL DLLMASDGSC QGVIALNMED GTLHRFRSSQ
TILATGGYGR AYFSATSAHT CTGDGNAMVA RAGLPLQDLE FVQFHPTGIY GAGCLITEGS
RGEGGILRNS EGERFMERYA PTAKDLASRD VVSRSMTMEI REGRGVGPHK DHIYLHLNHL
PPEVLKERLP GISETAAIFA GVDVTKEPIP VLPTVHYNMG GIPTNYHGEV VTIKGDDPDA
VIPGLMAAGE AACASVHGAN RLGANSLLDI VVFGRACANR VAEISKPGEK QKPLEKDAGE
KTIAWLDRLR NSNGSLPTST IRLNMQRIMQ NNAAVFRTQE TLEEGCQLID KAWESFGDVQ
VKDRSMIWNS DLIETLELEN LLINASITMH SAEARKESRG AHAREDFTKR EDGEWMKHTL
GYWEDEKVRL DYRPVHMDTL DDEIDTFPPK ARVY
//
