ID   DHSA1_ARATH             Reviewed;         634 AA.
AC   O82663;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 87.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial;
DE            EC=1.3.5.1;
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; 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   MEDLINE=20181125; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 160-170.
RC   TISSUE=Leaf, and Stem;
RX   MEDLINE=21608403; 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   [5]
RP   SUBUNIT, AND 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
RT   by 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 [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
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
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: a
CC       flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC       composed of a large and a small subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in
CC       flowers and inflorescences.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily.
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DR   EMBL; AJ001809; CAA05025.1; -; mRNA.
DR   EMBL; AB018119; BAA97282.1; -; 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   IPI; IPI00533552; -.
DR   PIR; T51815; T51815.
DR   RefSeq; NP_201477.1; -.
DR   UniGene; At.22655; -.
DR   UniGene; At.67108; -.
DR   HSSP; P10444; 1NEK.
DR   SMR; O82663; 41-634.
DR   PRIDE; O82663; -.
DR   GeneID; 836809; -.
DR   GenomeReviews; BA000015_GR; AT5G66760.
DR   KEGG; ath:AT5G66760; -.
DR   NMPDR; fig|3702.1.peg.28782; -.
DR   GeneFarm; 2175; 174.
DR   TAIR; At5g66760; -.
DR   OMA; O82663; EEDDWRW.
DR   BioCyc; MetaCyc:AT5G66760-MON; -.
DR   BRENDA; 1.3.5.1; 302.
DR   ArrayExpress; O82663; -.
DR   GermOnline; AT5G66760; Arabidopsis thaliana.
DR   GO; GO:0005618; C:cell wall; IDA:TAIR.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:TAIR.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; TAS:TAIR.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate...; TAS:TAIR.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR004112; Fum_Rdtase/Succ_DH_flav_C.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_frdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Electron transport; FAD;
KW   Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     32       Mitochondrion (Potential).
FT   CHAIN        33    634       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit 1, mitochondrial.
FT                                /FTId=PRO_0000158659.
FT   NP_BIND      79     94       FAD (By similarity).
FT   ACT_SITE    329    329       Proton acceptor (By similarity).
FT   BINDING     285    285       Substrate (By similarity).
FT   BINDING     297    297       Substrate (By similarity).
FT   BINDING     396    396       Substrate (By similarity).
FT   BINDING     441    441       Substrate (By similarity).
FT   MOD_RES      87     87       Tele-8alpha-FAD histidine (By
FT                                similarity).
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
//