SDHB2_ORYSJ
ID SDHB2_ORYSJ Reviewed; 311 AA.
AC Q6H4G3; A0A0P0XKU9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, 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=SDH2-2 {ECO:0000305};
GN OrderedLocusNames=Os09g0370300 {ECO:0000312|EMBL:BAF24932.1},
GN LOC_Os09g20440 {ECO:0000305};
GN ORFNames=B1168F12.7 {ECO:0000312|EMBL:BAD26386.1};
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 [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 [2]
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 [3]
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 [4]
RP 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}.
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DR EMBL; AP005872; BAD26386.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24932.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT07766.1; -; Genomic_DNA.
DR RefSeq; XP_015611366.1; XM_015755880.1.
DR AlphaFoldDB; Q6H4G3; -.
DR SMR; Q6H4G3; -.
DR STRING; 4530.OS09T0370300-01; -.
DR PaxDb; Q6H4G3; -.
DR PRIDE; Q6H4G3; -.
DR EnsemblPlants; Os09t0370300-01; Os09t0370300-01; Os09g0370300.
DR GeneID; 4346890; -.
DR Gramene; Os09t0370300-01; Os09t0370300-01; Os09g0370300.
DR KEGG; osa:4346890; -.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_3_1; -.
DR InParanoid; Q6H4G3; -.
DR OMA; CTHCYRC; -.
DR OrthoDB; 1264157at2759; -.
DR PlantReactome; R-OSA-1119533; TCA cycle (plant).
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q6H4G3; 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: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 Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
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; 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..63
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 64..311
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit 2, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431744"
FT DOMAIN 77..168
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 211..241
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 133
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 148
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 231
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 236
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 279
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 285
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 289
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
SQ SEQUENCE 311 AA; 34356 MW; A88DD8781F784FA3 CRC64;
MILRRTLPRL ASAKDGSGGG FADGHFPSLR GHPAARANAR DAAEKQAALA AKEEEIRDHR
RGDAAAASPA PSTVKEFRVY RWSPDAPSRR PHLQSYHVDL ATCGPMVLDV LQKIKAEHDA
TLAFRRSCRE GICGSCSMCI DGVNTVACLR PVDTDTSSAT TVTPLPHMYV VRDLVVDLTS
FYQQYKSVEP WLKRKTKTKT ETTEHAQSPE ERKRLDGLYE CILCACCSAA CPSYWWNAEA
FLGPAALLHA YRWVSDSRDE YAAERVQALA EGWDKLYRCR MIKSCTATCP KSLDPAAAIS
AMKTLHQLGK P
