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Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit 1 of complex II) (FP)

 SDHA1_ARATH             Reviewed;         634 AA.
O82663;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-APR-2018, entry version 155.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial;
EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
AltName: Full=Flavoprotein subunit 1 of complex II;
Short=FP;
Flags: Precursor;
Name=SDH1-1; OrderedLocusNames=At5g66760; ORFNames=MSN2.16;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. C24;
Machuy N., Klein M., Mueller-Roeber B.;
"Cloning and characterization of succinyl-CoA-ligase from Arabidopsis
thaliana.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
PROTEIN SEQUENCE OF 160-170.
TISSUE=Leaf, and Stem;
PubMed=11743114; DOI=10.1104/pp.127.4.1694;
Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
"Proteomic approach to identify novel mitochondrial proteins in
Arabidopsis.";
Plant Physiol. 127:1694-1710(2001).
[6]
TISSUE SPECIFICITY.
PubMed=12374303; DOI=10.1023/A:1019926301981;
Figueroa P., Leon G., Elorza A., Holuigue L., Araya A., Jordana X.;
"The four subunits of mitochondrial respiratory complex II are encoded
by multiple nuclear genes and targeted to mitochondria in Arabidopsis
thaliana.";
Plant Mol. Biol. 50:725-734(2002).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=14671022; DOI=10.1105/tpc.016055;
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome
highlights signaling and regulatory components, provides assessment of
targeting prediction programs, and indicates plant-specific
mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
PubMed=15604729; DOI=10.1007/s11103-004-2316-2;
Millar A.H., Eubel H., Jansch L., Kruft V., Heazlewood J.L.,
Braun H.P.;
"Mitochondrial cytochrome c oxidase and succinate dehydrogenase
complexes contain plant specific subunits.";
Plant Mol. Biol. 56:77-90(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE
AFTER PHE-32.
PubMed=25732537; DOI=10.1093/jxb/erv064;
Carrie C., Venne A.S., Zahedi R.P., Soll J.;
"Identification of cleavage sites and substrate proteins for two
mitochondrial intermediate peptidases in Arabidopsis thaliana.";
J. Exp. Bot. 66:2691-2708(2015).
-!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
(SDH) that is involved in complex II of the mitochondrial electron
transport chain and is responsible for transferring electrons from
succinate to ubiquinone (coenzyme Q).
{ECO:0000250|UniProtKB:P31040}.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000250|UniProtKB:P31040}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:Q0QF01};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000250|UniProtKB:P31040}.
-!- SUBUNIT: Component of complex II composed of eight subunits in
plants: four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a
flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
composed of a large and a small subunit.), as well as four
subunits unknown in mitochondria from bacteria and heterotrophic
eukaryotes. {ECO:0000269|PubMed:15604729}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537};
Peripheral membrane protein {ECO:0000269|PubMed:14671022}; Matrix
side {ECO:0000269|PubMed:14671022}.
-!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in
flowers and inflorescences. {ECO:0000269|PubMed:12374303}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
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EMBL; AJ001809; CAA05025.1; -; mRNA.
EMBL; AB018119; BAA97282.1; -; Genomic_DNA.
EMBL; CP002688; AED98260.1; -; Genomic_DNA.
EMBL; AF367341; AAK32928.1; -; mRNA.
EMBL; AY045674; AAK74032.1; -; mRNA.
EMBL; AF436833; AAL32015.1; -; mRNA.
EMBL; AY124812; AAM70521.1; -; mRNA.
PIR; T51815; T51815.
RefSeq; NP_201477.1; NM_126074.3.
UniGene; At.22655; -.
UniGene; At.67108; -.
ProteinModelPortal; O82663; -.
SMR; O82663; -.
BioGrid; 22051; 3.
IntAct; O82663; 2.
MINT; O82663; -.
STRING; 3702.AT5G66760.1; -.
SwissPalm; O82663; -.
PaxDb; O82663; -.
PRIDE; O82663; -.
EnsemblPlants; AT5G66760.1; AT5G66760.1; AT5G66760.
GeneID; 836809; -.
Gramene; AT5G66760.1; AT5G66760.1; AT5G66760.
KEGG; ath:AT5G66760; -.
Araport; AT5G66760; -.
TAIR; locus:2173654; AT5G66760.
eggNOG; KOG2403; Eukaryota.
eggNOG; COG1053; LUCA.
HOGENOM; HOG000160475; -.
InParanoid; O82663; -.
KO; K00234; -.
OMA; GDSPWEH; -.
OrthoDB; EOG093604YT; -.
PhylomeDB; O82663; -.
BioCyc; ARA:AT5G66760-MONOMER; -.
BioCyc; MetaCyc:AT5G66760-MONOMER; -.
UniPathway; UPA00223; UER01006.
PRO; PR:O82663; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; O82663; baseline and differential.
Genevisible; O82663; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:TAIR.
GO; GO:0050897; F:cobalt ion binding; IDA:TAIR.
GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
GO; GO:0000104; F:succinate dehydrogenase activity; TAS:TAIR.
GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; TAS:TAIR.
GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
Gene3D; 3.50.50.60; -; 2.
Gene3D; 3.90.700.10; -; 1.
InterPro; IPR003953; FAD-binding_2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR003952; FRD_SDH_FAD_BS.
InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
InterPro; IPR011281; Succ_DH_flav_su_fwd.
InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
Pfam; PF00890; FAD_binding_2; 1.
Pfam; PF02910; Succ_DH_flav_C; 1.
SUPFAM; SSF46977; SSF46977; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF56425; SSF56425; 1.
TIGRFAMs; TIGR01816; sdhA_forward; 1.
TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Electron transport; FAD;
Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
Oxidoreductase; Reference proteome; Transit peptide; Transport;
Tricarboxylic acid cycle.
TRANSIT 1 32 Mitochondrion.
{ECO:0000269|PubMed:25732537}.
CHAIN 33 634 Succinate dehydrogenase [ubiquinone]
flavoprotein subunit 1, mitochondrial.
/FTId=PRO_0000158659.
NP_BIND 56 61 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
NP_BIND 79 94 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
NP_BIND 446 447 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
ACT_SITE 329 329 Proton acceptor.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 264 264 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 285 285 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 297 297 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 396 396 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 430 430 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 441 441 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
MOD_RES 87 87 Tele-8alpha-FAD histidine.
{ECO:0000250|UniProtKB:Q9YHT1}.
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


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