SDHB3_ARATH
ID SDHB3_ARATH Reviewed; 309 AA.
AC Q9FJP9; Q9G3L8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 3, mitochondrial;
DE EC=1.3.5.1;
DE AltName: Full=Iron-sulfur subunit of complex II;
DE Short=Ip;
DE Flags: Precursor;
GN Name=SDH2-3; OrderedLocusNames=At5g65165; ORFNames=MQN23.10;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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 DEVELOPMENTAL STAGE.
RX PubMed=16249327; DOI=10.1093/pcp/pci218;
RA Elorza A., Roschzttardtz H., Gomez I., Mouras A., Holuigue L., Araya A.,
RA Jordana X.;
RT "A nuclear gene for the iron-sulfur subunit of mitochondrial complex II is
RT specifically expressed during Arabidopsis seed development and
RT germination.";
RL Plant Cell Physiol. 47:14-21(2006).
RN [5]
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).
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 {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed development. Detected during
CC seed maturation and decreased during germination.
CC {ECO:0000269|PubMed:16249327}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; AJ278912; CAC19857.1; -; mRNA.
DR EMBL; AB013395; BAB11652.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98011.1; -; Genomic_DNA.
DR RefSeq; NP_680465.2; NM_148160.3.
DR AlphaFoldDB; Q9FJP9; -.
DR SMR; Q9FJP9; -.
DR BioGRID; 21882; 6.
DR STRING; 3702.AT5G65165.1; -.
DR PaxDb; Q9FJP9; -.
DR PRIDE; Q9FJP9; -.
DR ProteomicsDB; 232778; -.
DR EnsemblPlants; AT5G65165.1; AT5G65165.1; AT5G65165.
DR GeneID; 836640; -.
DR Gramene; AT5G65165.1; AT5G65165.1; AT5G65165.
DR KEGG; ath:AT5G65165; -.
DR Araport; AT5G65165; -.
DR TAIR; locus:504954878; AT5G65165.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_3_1; -.
DR InParanoid; Q9FJP9; -.
DR OMA; CTHCYRC; -.
DR OrthoDB; 1264157at2759; -.
DR PhylomeDB; Q9FJP9; -.
DR UniPathway; UPA00223; UER01006.
DR PRO; PR:Q9FJP9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJP9; baseline and differential.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 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..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..309
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit 3, mitochondrial"
FT /id="PRO_0000247597"
FT DOMAIN 69..160
FT /note="2Fe-2S ferredoxin-type"
FT DOMAIN 202..232
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 125
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 212
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 222
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 227
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 270
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 276
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P07014"
FT BINDING 280
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P07014"
SQ SEQUENCE 309 AA; 34983 MW; F69189C234D87A1D CRC64;
MSSVLRLLGR RICNPAAEKV RLSSSLSGGG DFPILNGHKA AQDLSKDTLK SQDITKEKEG
QHKEVKKEFK IYRWNPDKPN SKPFLQSFFV DLSSCGPMVL DVLQKIKAED DASLSYRRSC
REGICGSCSM NIDGTNTVAC LKPINPNTSK PTIITPLPHM YVIKDLVVDL TNFYQQYKSM
EPWLKTRKPP KDGREHRQSP KDRKKLDGLY ECILCACCTT SCPSYWWNPE EFPGPAALLQ
AYRWISDSRD EYREERLQAI TESETKVYRC RAIKNCTATC PKGLNPASAI LKMKSKHLLS
DPLVRTESV
