SDHB2_ARATH
ID SDHB2_ARATH Reviewed; 280 AA.
AC Q8LB02; Q9FM32; Q9G3L9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial;
DE EC=1.3.5.1;
DE AltName: Full=Iron-sulfur subunit of complex II;
DE Short=Ip;
DE Flags: Precursor;
GN Name=SDH2-2; OrderedLocusNames=At5g40650; ORFNames=MNF13.170, MNF13.21;
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], 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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 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 [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.
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 [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 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., 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 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). {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:190135;
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; fumarate
CC from succinate (eukaryal route): step 1/1. {ECO:0000305}.
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: Ubiquitous. Preferentially expressed in flowers,
CC inflorescences and root tips. {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 anthers,
CC particularly in the tapetum, pollen mother cells, and microspores.
CC {ECO:0000269|PubMed:15563621}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; AJ278911; CAC19856.1; -; mRNA.
DR EMBL; AB009052; BAB08537.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94578.1; -; Genomic_DNA.
DR EMBL; AY074299; AAL66996.1; -; mRNA.
DR EMBL; AY123036; AAM67569.1; -; mRNA.
DR EMBL; AY087504; AAM65047.1; -; mRNA.
DR RefSeq; NP_198881.1; NM_123430.2.
DR AlphaFoldDB; Q8LB02; -.
DR SMR; Q8LB02; -.
DR BioGRID; 19316; 7.
DR IntAct; Q8LB02; 1.
DR STRING; 3702.AT5G40650.1; -.
DR SwissPalm; Q8LB02; -.
DR PaxDb; Q8LB02; -.
DR PRIDE; Q8LB02; -.
DR ProteomicsDB; 232888; -.
DR EnsemblPlants; AT5G40650.1; AT5G40650.1; AT5G40650.
DR GeneID; 834065; -.
DR Gramene; AT5G40650.1; AT5G40650.1; AT5G40650.
DR KEGG; ath:AT5G40650; -.
DR Araport; AT5G40650; -.
DR TAIR; locus:2168818; AT5G40650.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_2_1; -.
DR InParanoid; Q8LB02; -.
DR OMA; DGQYFGP; -.
DR OrthoDB; 1264157at2759; -.
DR PhylomeDB; Q8LB02; -.
DR BioCyc; ARA:AT5G40650-MON; -.
DR BioCyc; MetaCyc:AT5G40650-MON; -.
DR BRENDA; 1.3.5.1; 399.
DR UniPathway; UPA00223; UER01006.
DR PRO; PR:Q8LB02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LB02; baseline and differential.
DR Genevisible; Q8LB02; 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:0009536; C:plastid; HDA: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; HDA: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; 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; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..280
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit 2, mitochondrial"
FT /id="PRO_0000247596"
FT DOMAIN 51..140
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 183..213
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 106
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 121
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 203
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 208
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with SdhD subunit"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 250
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 256
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT CONFLICT 14
FT /note="S -> P (in Ref. 1; CAC19856 and 5; AAM65047)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="T -> K (in Ref. 1; CAC19856 and 5; AAM65047)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="S -> F (in Ref. 1; CAC19856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31141 MW; 1F505A8C7D68DACD CRC64;
MAFGLIGRVV GTKSSRLSTA ARLIPARWTS TGSEAQSKAS TGGGGASLKT FQIYRWNPDN
PGKPELQDYK IDLKDCGPMV LDALIKIKNE MDPSLTFRRS CREGICGSCA MNIDGCNGLA
CLTKIESGSK ETTITPLPHM FVIKDLVVDM TNFYNQYKSI EPWLKRKNPA SVPGKEILQS
KKDRAKLDGM YECILCACCS TSCPSYWWNP ESYLGPAALL HANRWISDSR DEYTKERLEA
IDDEFKLYRC HTILNCARAC PKGLNPGKQI THIKQLQKSG
