SDHB_PIG
ID SDHB_PIG Reviewed; 280 AA.
AC Q007T0; Q0QEX6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-264.
RC TISSUE=Liver;
RX PubMed=16751257; DOI=10.1093/molbev/msl027;
RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL Mol. Biol. Evol. 23:1493-1503(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-279 IN COMPLEX WITH IRON-SULFUR
RP CLUSTERS AND UBIQUINONE, AND SUBUNIT.
RX PubMed=15989954; DOI=10.1016/j.cell.2005.05.025;
RA Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.;
RT "Crystal structure of mitochondrial respiratory membrane protein complex
RT II.";
RL Cell 121:1043-1057(2005).
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 (PubMed:15989954). Interacts with
CC SDHAF1; the interaction is required for iron-sulfur cluster
CC incorporation into SDHB (By similarity). {ECO:0000250|UniProtKB:P21912,
CC ECO:0000269|PubMed:15989954}.
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; DQ915498; ABJ09403.1; -; mRNA.
DR EMBL; DQ403018; ABD77151.1; -; mRNA.
DR RefSeq; NP_001098423.1; NM_001104953.1.
DR PDB; 1ZOY; X-ray; 2.40 A; B=29-279.
DR PDB; 1ZP0; X-ray; 3.50 A; B=29-279.
DR PDB; 3ABV; X-ray; 3.24 A; B=29-280.
DR PDB; 3AE1; X-ray; 3.14 A; B=29-280.
DR PDB; 3AE2; X-ray; 3.10 A; B=29-280.
DR PDB; 3AE3; X-ray; 3.35 A; B=29-280.
DR PDB; 3AE4; X-ray; 2.91 A; B=29-280.
DR PDB; 3AE5; X-ray; 3.41 A; B=29-280.
DR PDB; 3AE6; X-ray; 3.40 A; B=29-280.
DR PDB; 3AE7; X-ray; 3.62 A; B=29-280.
DR PDB; 3AE8; X-ray; 3.40 A; B=29-280.
DR PDB; 3AE9; X-ray; 3.31 A; B=29-280.
DR PDB; 3AEA; X-ray; 3.39 A; B=29-280.
DR PDB; 3AEB; X-ray; 3.00 A; B=29-280.
DR PDB; 3AEC; X-ray; 3.61 A; B=29-280.
DR PDB; 3AED; X-ray; 3.52 A; B=29-280.
DR PDB; 3AEE; X-ray; 3.22 A; B=29-280.
DR PDB; 3AEF; X-ray; 2.80 A; B=29-280.
DR PDB; 3AEG; X-ray; 3.27 A; B=29-280.
DR PDB; 3SFD; X-ray; 2.61 A; B=29-280.
DR PDB; 3SFE; X-ray; 2.81 A; B=29-280.
DR PDB; 4YTP; X-ray; 3.10 A; B=1-280.
DR PDB; 4YXD; X-ray; 3.00 A; B=1-280.
DR PDBsum; 1ZOY; -.
DR PDBsum; 1ZP0; -.
DR PDBsum; 3ABV; -.
DR PDBsum; 3AE1; -.
DR PDBsum; 3AE2; -.
DR PDBsum; 3AE3; -.
DR PDBsum; 3AE4; -.
DR PDBsum; 3AE5; -.
DR PDBsum; 3AE6; -.
DR PDBsum; 3AE7; -.
DR PDBsum; 3AE8; -.
DR PDBsum; 3AE9; -.
DR PDBsum; 3AEA; -.
DR PDBsum; 3AEB; -.
DR PDBsum; 3AEC; -.
DR PDBsum; 3AED; -.
DR PDBsum; 3AEE; -.
DR PDBsum; 3AEF; -.
DR PDBsum; 3AEG; -.
DR PDBsum; 3SFD; -.
DR PDBsum; 3SFE; -.
DR PDBsum; 4YTP; -.
DR PDBsum; 4YXD; -.
DR AlphaFoldDB; Q007T0; -.
DR SMR; Q007T0; -.
DR STRING; 9823.ENSSSCP00000022052; -.
DR ChEMBL; CHEMBL2366485; -.
DR PaxDb; Q007T0; -.
DR PeptideAtlas; Q007T0; -.
DR PRIDE; Q007T0; -.
DR GeneID; 414412; -.
DR KEGG; ssc:414412; -.
DR CTD; 6390; -.
DR eggNOG; KOG3049; Eukaryota.
DR InParanoid; Q007T0; -.
DR OrthoDB; 1264157at2759; -.
DR UniPathway; UPA00223; UER01006.
DR EvolutionaryTrace; Q007T0; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA: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; IDA: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; Acetylation; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT CHAIN 29..280
FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT subunit, mitochondrial"
FT /id="PRO_0000343799"
FT DOMAIN 40..131
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 BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 196
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT BINDING 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with DHSD"
FT /evidence="ECO:0000269|PubMed:15989954"
FT BINDING 243
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT BINDING 249
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT BINDING 253
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
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"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3SFD"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1ZOY"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3AEF"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:1ZOY"
FT TURN 163..167
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1ZOY"
FT TURN 179..185
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:1ZOY"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1ZOY"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1ZOY"
SQ SEQUENCE 280 AA; 31586 MW; 096B11189EF1ED59 CRC64;
MAAVVAVSLK RWFPATTLGG ACLQACRGAQ TAAATAPRIK KFAIYRWDPD KTGDKPHMQT
YEIDLNNCGP MVLDALIKIK NEIDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN
LDKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQEGKQQY LQSIEEREKL
DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL
YRCHTIMNCT GTCPKGLNPG KAIAEIKKMM ATYKEKKASA
