SDHB_CHOCR
ID SDHB_CHOCR Reviewed; 250 AA.
AC P48932;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit;
DE EC=1.3.5.1;
DE AltName: Full=Iron-sulfur subunit of complex II;
DE Short=Ip;
GN Name=SDH2; Synonyms=SDHB;
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OG Mitochondrion.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8821668; DOI=10.1007/bf02221585;
RA Viehmann S., Richard O., Boyen C., Zetsche K.;
RT "Genes for two subunits of succinate dehydrogenase form a cluster on the
RT mitochondrial genome of Rhodophyta.";
RL Curr. Genet. 29:199-201(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Apices;
RX PubMed=7616569; DOI=10.1006/jmbi.1995.0392;
RA Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M.,
RA Kloareg B.;
RT "Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus
RT crispus (Gigartinales). Gene content and genome organization.";
RL J. Mol. Biol. 250:484-495(1995).
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; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC -!- SUBUNIT: Component of complex II composed of four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC composed of a large and a small subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; Z47547; CAA87611.1; -; Genomic_DNA.
DR PIR; S59114; S59114.
DR RefSeq; NP_062488.1; NC_001677.2.
DR AlphaFoldDB; P48932; -.
DR SMR; P48932; -.
DR GeneID; 809396; -.
DR KEGG; ccp:ChcroMp09; -.
DR UniPathway; UPA00223; UER01006.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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: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 3: Inferred from homology;
KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Transport; Tricarboxylic acid cycle.
FT CHAIN 1..250
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit"
FT /id="PRO_0000158694"
FT DOMAIN 30..110
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 153..183
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with DHSD"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 28887 MW; 09511AE52A4CA149 CRC64;
MIIKNLNQKI ITIDNSSPYQ KFIRIYRWNP NLNLNPWFSI FPISTNNCGP MILDALIQIK
NIQDSSLTFR RSCREGICGS CSMNIDGTNS LACLRSLNTK SNFITIYPLP HTYIIKDLVP
DLSNFYAQYK LIKPWLINKI GFSLKENLQS KIDRLELDGL YECILCACCS ASCPSYWWNQ
DKYLGPAILL QAYRWIVDSR DNSTENRLNF LNNKMRLFRC HTIMNCSKTC PKSLNPGKAI
ASIKYRIINN
