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Database: UniProt
Entry: Q8LBZ7
LinkDB: Q8LBZ7
Original site: Q8LBZ7 
ID   SDHB1_ARATH             Reviewed;         279 AA.
AC   Q8LBZ7; Q9G3M0; Q9LTZ2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   10-APR-2019, entry version 128.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 1, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II;
DE            Short=Ip;
DE   Flags: Precursor;
GN   Name=SDH2-1; OrderedLocusNames=At3g27380; ORFNames=K1G2.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11442063; DOI=10.1023/A:1010612506070;
RA   Figueroa P., Leon G., Elorza A., Holuigue L., Jordana X.;
RT   "Three different genes encode the iron-sulphur subunit of succinate
RT   dehydrogenase in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 46:241-250(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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
RT   reference 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.,
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE 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
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).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12970493; DOI=10.1104/pp.103.024620;
RA   Eubel H., Jansch L., Braun H.P.;
RT   "New insights into the respiratory chain of plant mitochondria.
RT   Supercomplexes and a unique composition of complex II.";
RL   Plant Physiol. 133:274-286(2003).
RN   [9]
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.,
RA   Braun H.P.;
RT   "Mitochondrial cytochrome c oxidase and succinate dehydrogenase
RT   complexes contain plant specific subunits.";
RL   Plant Mol. Biol. 56:77-90(2004).
RN   [10]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=15563621; DOI=10.1104/pp.104.049528;
RA   Elorza A., Leon G., Gomez I., Mouras A., Holuigue L., Araya A.,
RA   Jordana X.;
RT   "Nuclear SDH2-1 and SDH2-2 genes, encoding the iron-sulfur subunit of
RT   mitochondrial complex II in Arabidopsis, have distinct cell-specific
RT   expression patterns and promoter activities.";
RL   Plant Physiol. 136:4072-4087(2004).
CC   -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate
CC       dehydrogenase (SDH) that is involved in complex II of the
CC       mitochondrial electron transport chain and is responsible for
CC       transferring electrons from succinate to ubiquinone (coenzyme Q).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250|UniProtKB:P07014};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P07014};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250|UniProtKB:P07014};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P07014};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P07014};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P07014};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Component of complex II composed of eight subunits in
CC       plants: four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a
CC       flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC       composed of a large and a small subunit.), as well as four
CC       subunits unknown in mitochondria from bacteria and heterotrophic
CC       eukaryotes. {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: Ubiquitous. Preferentially expressed in
CC       flowers and inflorescences. {ECO:0000269|PubMed:11442063,
CC       ECO:0000269|PubMed:15563621}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in floral meristems and sex organ
CC       primordia at early stages of development. Later expressed in
CC       anthers, particularly in the tapetum, pollen mother cells, and
CC       microspores. {ECO:0000269|PubMed:15563621}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; AJ278910; CAC19855.1; -; mRNA.
DR   EMBL; AB024028; BAA95713.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77309.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77310.1; -; Genomic_DNA.
DR   EMBL; AY035013; AAK59518.1; -; mRNA.
DR   EMBL; AY063053; AAL34227.1; -; mRNA.
DR   EMBL; AY924777; AAX23852.1; -; mRNA.
DR   EMBL; AY086901; AAM63946.1; -; mRNA.
DR   RefSeq; NP_001118718.1; NM_001125246.1.
DR   RefSeq; NP_189374.1; NM_113653.4.
DR   UniGene; At.17610; -.
DR   UniGene; At.22540; -.
DR   UniGene; At.32384; -.
DR   UniGene; At.71559; -.
DR   ProteinModelPortal; Q8LBZ7; -.
DR   SMR; Q8LBZ7; -.
DR   BioGrid; 7689; 3.
DR   IntAct; Q8LBZ7; 2.
DR   MINT; Q8LBZ7; -.
DR   STRING; 3702.AT3G27380.2; -.
DR   PaxDb; Q8LBZ7; -.
DR   PRIDE; Q8LBZ7; -.
DR   EnsemblPlants; AT3G27380.1; AT3G27380.1; AT3G27380.
DR   EnsemblPlants; AT3G27380.2; AT3G27380.2; AT3G27380.
DR   GeneID; 822359; -.
DR   Gramene; AT3G27380.1; AT3G27380.1; AT3G27380.
DR   Gramene; AT3G27380.2; AT3G27380.2; AT3G27380.
DR   KEGG; ath:AT3G27380; -.
DR   Araport; AT3G27380; -.
DR   TAIR; locus:2086716; AT3G27380.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   HOGENOM; HOG000160590; -.
DR   InParanoid; Q8LBZ7; -.
DR   KO; K00235; -.
DR   OMA; FQIYRWT; -.
DR   OrthoDB; 1264157at2759; -.
DR   PhylomeDB; Q8LBZ7; -.
DR   BRENDA; 1.3.5.1; 399.
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:Q8LBZ7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LBZ7; baseline and differential.
DR   Genevisible; Q8LBZ7; AT.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
DR   GO; GO:0045281; C:succinate dehydrogenase complex; ISS:TAIR.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; ISS:TAIR.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; ISS:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:TAIR.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   Pfam; PF13085; Fer2_3; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     28       Mitochondrion. {ECO:0000255}.
FT   CHAIN        29    279       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit 1, mitochondrial.
FT                                /FTId=PRO_0000247595.
FT   DOMAIN       52    141       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      184    214       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       102    102       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       107    107       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       122    122       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       194    194       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       197    197       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       200    200       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       204    204       Iron-sulfur 3 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       251    251       Iron-sulfur 3 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       257    257       Iron-sulfur 3 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   METAL       261    261       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   BINDING     209    209       Ubiquinone; shared with SdhD subunit.
FT                                {ECO:0000250|UniProtKB:P07014}.
FT   CONFLICT     20     20       A -> V (in Ref. 1; CAC19855 and 6;
FT                                AAM63946). {ECO:0000305}.
FT   CONFLICT     26     26       A -> V (in Ref. 1; CAC19855 and 6;
FT                                AAM63946). {ECO:0000305}.
FT   CONFLICT    200    200       C -> F (in Ref. 6; AAM63946).
FT                                {ECO:0000305}.
SQ   SEQUENCE   279 AA;  31171 MW;  ADA885EC59A3EA36 CRC64;
     MASGLIGRLV GTKPSKLATA ARLIPARWTS TGAEAETKAS SGGGRGSNLK TFQIYRWNPD
     NPGKPELQNY QIDLKDCGPM VLDALIKIKN EMDPSLTFRR SCREGICGSC AMNIDGCNGL
     ACLTKIQDEA SETTITPLPH MFVIKDLVVD MTNFYNQYKS IEPWLKRKTP ASVPAKEILQ
     SKKDRAKLDG MYECILCACC STSCPSYWWN PESYLGPAAL LHANRWISDS RDEYTKERLE
     AIDDEFKLYR CHTILNCARA CPKGLNPGKQ ITHIKQLQR
//
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