ID SDHB1_ORYSJ Reviewed; 281 AA.
AC Q9S827; A0A0N7KP69;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 1, mitochondrial;
DE EC=1.3.5.1 {ECO:0000305};
DE AltName: Full=Iron-sulfur subunit of complex II;
DE Short=Ip;
DE Flags: Precursor;
GN Name=SDH2-1 {ECO:0000305};
GN OrderedLocusNames=Os08g0120000 {ECO:0000312|EMBL:BAF22790.1},
GN LOC_Os08g02640 {ECO:0000305};
GN ORFNames=OJ1005_B05.29-1 {ECO:0000312|EMBL:BAD09055.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Nohrin 8; TISSUE=Seedling;
RX PubMed=10430921; DOI=10.1073/pnas.96.16.9207;
RA Kubo N., Harada K., Hirai A., Kadowaki K.;
RT "A single nuclear transcript encoding mitochondrial RPS14 and SDHB of rice
RT is processed by alternative splicing: common use of the same mitochondrial
RT targeting signal for different proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9207-9211(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP PROTEIN SEQUENCE OF 226-231 AND 237-247, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBUNIT.
RX PubMed=19924544; DOI=10.1007/s11103-009-9573-z;
RA Huang S., Taylor N.L., Narsai R., Eubel H., Whelan J., Millar A.H.;
RT "Functional and composition differences between mitochondrial complex II in
RT Arabidopsis and rice are correlated with the complex genetic history of the
RT enzyme.";
RL Plant Mol. Biol. 72:331-342(2010).
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|UniProtKB:Q8LBZ7}.
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:0000305};
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:19924544}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8LBZ7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8LBZ7}; Matrix side
CC {ECO:0000250|UniProtKB:Q8LBZ7}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017428; BAA82749.1; -; mRNA.
DR EMBL; AB017429; BAA82750.1; -; Genomic_DNA.
DR EMBL; AP003925; BAD09055.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22790.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03586.1; -; Genomic_DNA.
DR EMBL; AK059815; BAG87144.1; -; mRNA.
DR EMBL; AK104303; BAG96585.1; -; mRNA.
DR EMBL; AK104304; BAG96586.1; -; mRNA.
DR RefSeq; XP_015650211.1; XM_015794725.1.
DR RefSeq; XP_015650213.1; XM_015794727.1.
DR AlphaFoldDB; Q9S827; -.
DR SMR; Q9S827; -.
DR STRING; 39947.Q9S827; -.
DR PaxDb; 39947-Q9S827; -.
DR EnsemblPlants; Os08t0120000-01; Os08t0120000-01; Os08g0120000.
DR EnsemblPlants; Os08t0120000-02; Os08t0120000-02; Os08g0120000.
DR EnsemblPlants; Os08t0120000-04; Os08t0120000-04; Os08g0120000.
DR GeneID; 4344541; -.
DR Gramene; Os08t0120000-01; Os08t0120000-01; Os08g0120000.
DR Gramene; Os08t0120000-02; Os08t0120000-02; Os08g0120000.
DR Gramene; Os08t0120000-04; Os08t0120000-04; Os08g0120000.
DR KEGG; osa:4344541; -.
DR eggNOG; KOG1741; Eukaryota.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_1_1; -.
DR InParanoid; Q9S827; -.
DR OMA; CSTVAFR; -.
DR OrthoDB; 119960at2759; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q9S827; baseline and differential.
DR Genevisible; Q9S827; OS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
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; 3.10.20.30; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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 NCBIfam; TIGR00384; dhsB; 1.
DR PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR Pfam; PF13085; Fer2_3; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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; Direct protein sequencing; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..281
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit 1, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431743"
FT DOMAIN 49..141
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 184..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 122
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 200
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 204
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 209
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 251
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 257
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
SQ SEQUENCE 281 AA; 31119 MW; 0F90201DB967121B CRC64;
MAAAALLRRS PAARALLSPA LSSRLVASKP HSSSPAPPPP PSKAGANTKT FSIYRWDPDS
PSTKPHLKDY KVDLSDCGPM VLDVLLKIKN EQDPSLTFRR SCREGICGSC AMNIDGDNGL
ACLTKISSAS SASTISPLPH MFVIKDLVVD MTNFYNQYKS VEPWLKRKDA PPQPGKEIPQ
TKADRAKLDG MYECILCACC STSCPSYWWN PEEYLGPAAL LHANRWIQDS RDQFTKERLD
SINDEFKLYR CHTIKNCTHA CPKGLNPAKH IDTIKKLQLE A
//
