SDHB_CHICK
ID SDHB_CHICK Reviewed; 290 AA.
AC Q9YHT2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Weinreich D.M.;
RT "OXPHOS genes in mammals and the molecular clock.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 39-290, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15805592; DOI=10.1107/s0907444905000181;
RA Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.;
RT "Crystallization of mitochondrial respiratory complex II from chicken
RT heart: a membrane-protein complex diffracting to 2.0 A.";
RL Acta Crystallogr. D 61:380-387(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 39-290 IN COMPLEX WITH UBIQUINONE
RP AND IRON-SULFUR CENTERS, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16935256; DOI=10.1016/j.bbabio.2006.06.015;
RA Huang L.-S., Shen J.T., Wang A.C., Berry E.A.;
RT "Crystallographic studies of the binding of ligands to the dicarboxylate
RT site of complex II, and the identity of the ligand in the 'oxaloacetate-
RT inhibited' state.";
RL Biochim. Biophys. Acta 1757:1073-1083(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-290 IN COMPLEX WITH UBIQUINONE
RP AND IRON-SULFUR CENTERS, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16371358; DOI=10.1074/jbc.m511270200;
RA Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y.,
RA Anderson V.E., Berry E.A.;
RT "3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration
RT that, upon oxidation by complex II, forms a covalent adduct with a
RT catalytic base arginine in the active site of the enzyme.";
RL J. Biol. Chem. 281:5965-5972(2006).
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;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Note=Binds 1 [3Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
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. {ECO:0000269|PubMed:15805592,
CC ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC ECO:0000269|PubMed:16935256}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC ECO:0000269|PubMed:16935256}; Matrix side {ECO:0000269|PubMed:15805592,
CC ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000305}.
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DR EMBL; AF095937; AAC72372.1; -; mRNA.
DR PDB; 1YQ3; X-ray; 2.20 A; B=39-290.
DR PDB; 1YQ4; X-ray; 2.33 A; B=39-290.
DR PDB; 2FBW; X-ray; 2.10 A; B/O=39-290.
DR PDB; 2H88; X-ray; 1.74 A; B/O=39-290.
DR PDB; 2H89; X-ray; 2.40 A; B=39-290.
DR PDB; 2WQY; X-ray; 2.10 A; B/O=39-290.
DR PDB; 6MYO; X-ray; 2.20 A; B=39-290.
DR PDB; 6MYP; X-ray; 2.10 A; B=39-290.
DR PDB; 6MYQ; X-ray; 1.97 A; B=39-290.
DR PDB; 6MYR; X-ray; 2.15 A; B=39-290.
DR PDB; 6MYS; X-ray; 2.37 A; B=39-290.
DR PDB; 6MYT; X-ray; 2.27 A; B=39-290.
DR PDB; 6MYU; X-ray; 1.97 A; B=39-290.
DR PDBsum; 1YQ3; -.
DR PDBsum; 1YQ4; -.
DR PDBsum; 2FBW; -.
DR PDBsum; 2H88; -.
DR PDBsum; 2H89; -.
DR PDBsum; 2WQY; -.
DR PDBsum; 6MYO; -.
DR PDBsum; 6MYP; -.
DR PDBsum; 6MYQ; -.
DR PDBsum; 6MYR; -.
DR PDBsum; 6MYS; -.
DR PDBsum; 6MYT; -.
DR PDBsum; 6MYU; -.
DR AlphaFoldDB; Q9YHT2; -.
DR SMR; Q9YHT2; -.
DR STRING; 9031.ENSGALP00000000693; -.
DR PaxDb; Q9YHT2; -.
DR VEuPathDB; HostDB:geneid_100859720; -.
DR eggNOG; KOG3049; Eukaryota.
DR InParanoid; Q9YHT2; -.
DR PhylomeDB; Q9YHT2; -.
DR Reactome; R-GGA-372987; The tricarboxylic acid cycle.
DR UniPathway; UPA00223; UER01006.
DR EvolutionaryTrace; Q9YHT2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
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: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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT CHAIN 39..290
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit, mitochondrial"
FT /id="PRO_0000343800"
FT DOMAIN 50..143
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 186..216
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 206
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT BINDING 211
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with DHSD"
FT /evidence="ECO:0000269|PubMed:16371358,
FT ECO:0000269|PubMed:16935256"
FT BINDING 253
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT BINDING 259
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2H88"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2H88"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2H88"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2H88"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2H88"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2H88"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1YQ4"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:2H88"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:2H88"
FT TURN 189..195
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:2H88"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:2H88"
FT TURN 247..252
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:2H88"
SQ SEQUENCE 290 AA; 32597 MW; 313E698866B3FDFC CRC64;
MAAAVVGVSL RRGVPARFLR AGLRPVRGLE AVHGICRGAQ TAAAATSRIK KFSIYRWDPD
KPGDKPRMQT YEVDLNKCGP MVLDALIKIK NELDSTLTFR RSCREGICGS CAMNIAGGNT
LACTKKIDPD LSKTTKIYPL PHMYVVKDLV PDLSNFYAQY KSIEPYLKKK DESKQGKEQY
LQSIEDRQKL DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDYTEER
LAQLQDPFSL YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKAAAA
