SDHB_BOVIN
ID SDHB_BOVIN Reviewed; 280 AA.
AC Q3T189;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;
DE EC=1.3.5.1;
DE AltName: Full=Iron-sulfur subunit of complex II;
DE Short=IP;
DE Flags: Precursor;
GN Name=SDHB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Iron-sulfur protein (IP) subunit of the succinate
CC dehydrogenase complex (mitochondrial respiratory chain complex II),
CC responsible for transferring electrons from succinate to ubiquinone
CC (coenzyme Q). {ECO:0000250|UniProtKB:P21912}.
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: the
CC flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome
CC b560 composed of SDHC and SDHD (By similarity). Interacts with SDHAF1;
CC the interaction is required for iron-sulfur cluster incorporation into
CC SDHB (By similarity). {ECO:0000250|UniProtKB:P21912,
CC ECO:0000250|UniProtKB:Q007T0}.
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}.
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; BC102067; AAI02068.1; -; mRNA.
DR RefSeq; NP_001035573.1; NM_001040483.1.
DR AlphaFoldDB; Q3T189; -.
DR SMR; Q3T189; -.
DR CORUM; Q3T189; -.
DR IntAct; Q3T189; 2.
DR STRING; 9913.ENSBTAP00000010949; -.
DR PaxDb; Q3T189; -.
DR PeptideAtlas; Q3T189; -.
DR PRIDE; Q3T189; -.
DR GeneID; 286840; -.
DR KEGG; bta:286840; -.
DR CTD; 6390; -.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_2_1; -.
DR InParanoid; Q3T189; -.
DR OrthoDB; 1264157at2759; -.
DR TreeFam; TF300754; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
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:0048039; F:ubiquinone binding; ISS:UniProtKB.
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; 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 2: Evidence at transcript level;
KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Acetylation; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Oxidoreductase; Reference proteome; Transit peptide; Transport;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..280
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit, mitochondrial"
FT /id="PRO_0000247594"
FT DOMAIN 40..133
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 176..206
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 146..218
FT /note="Interaction with SDHAF1"
FT /evidence="ECO:0000250|UniProtKB:P21912"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with DHSD"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQA3"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQA3"
SQ SEQUENCE 280 AA; 31518 MW; BE51FF2193F8B6C5 CRC64;
MAAVVALSLR RRFPAAALGG ARLQACRGAQ TAAAAAPRIK KFAIYRWDPD KTGDKPHMQT
YEIDLNNCGP MVLDALIKIK NEIDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN
LSKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQGGKEQY LQSIEDREKL
DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL
YRCHTIMNCT QTCPKGLNPG KAIAEIKKMM ATYKEKQASA
