DHSD_ECOLI
ID DHSD_ECOLI Reviewed; 115 AA.
AC P0AC44; P10445;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN Name=sdhD; OrderedLocusNames=b0722, JW0712;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6383359; DOI=10.1042/bj2220519;
RA Wood D., Darlison M.G., Wilde R.J., Guest J.R.;
RT "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of
RT the succinate dehydrogenase of Escherichia coli.";
RL Biochem. J. 222:519-534(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP MUTAGENESIS OF HISTIDINE RESIDUES.
RX PubMed=9521736; DOI=10.1021/bi9716635;
RA Vibat C.R., Cecchini G., Nakamura K., Kita K., Gennis R.B.;
RT "Localization of histidine residues responsible for heme axial ligation in
RT cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in
RT Escherichia coli.";
RL Biochemistry 37:4148-4159(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HEME AND UBIQUINONE,
RP SUBUNIT, AND TRANSMEMBRANE TOPOLOGY.
RX PubMed=12560550; DOI=10.1126/science.1079605;
RA Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H.,
RA Leger C., Byrne B., Cecchini G., Iwata S.;
RT "Architecture of succinate dehydrogenase and reactive oxygen species
RT generation.";
RL Science 299:700-704(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT, AND
RP TRANSMEMBRANE TOPOLOGY.
RX PubMed=16407191; DOI=10.1074/jbc.m508173200;
RA Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K.,
RA Omura S., Byrne B., Cecchini G., Iwata S.;
RT "Structural and computational analysis of the quinone-binding site of
RT complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron
RT transfer and proton conduction during ubiquinone reduction.";
RL J. Biol. Chem. 281:7309-7316(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT, AND
RP TRANSMEMBRANE TOPOLOGY.
RX PubMed=19710024; DOI=10.1074/jbc.m109.010058;
RA Ruprecht J., Yankovskaya V., Maklashina E., Iwata S., Cecchini G.;
RT "Structure of Escherichia coli succinate:quinone oxidoreductase with an
RT occupied and empty quinone-binding site.";
RL J. Biol. Chem. 284:29836-29846(2009).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=The heme is bound between the two transmembrane subunits.;
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur protein, plus two membrane-anchoring
CC proteins, SdhC and SdhD. The complex can form homotrimers.
CC {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191,
CC ECO:0000269|PubMed:19710024}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
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; J01619; AAA23894.1; -; Genomic_DNA.
DR EMBL; X00980; CAA25486.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73816.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35389.1; -; Genomic_DNA.
DR PIR; B28836; DEECS2.
DR RefSeq; NP_415250.1; NC_000913.3.
DR RefSeq; WP_000254365.1; NZ_STEB01000035.1.
DR PDB; 1NEK; X-ray; 2.60 A; D=1-115.
DR PDB; 1NEN; X-ray; 2.90 A; D=1-115.
DR PDB; 2ACZ; X-ray; 3.10 A; D=1-115.
DR PDB; 2WDQ; X-ray; 2.40 A; D/H/L=1-115.
DR PDB; 2WDR; X-ray; 3.20 A; D/H/L=1-115.
DR PDB; 2WDV; X-ray; 3.20 A; D/H/L=1-115.
DR PDB; 2WP9; X-ray; 2.70 A; D/H/L=1-115.
DR PDB; 2WS3; X-ray; 3.20 A; D/H/L=1-115.
DR PDB; 2WU2; X-ray; 2.50 A; D/H/L=1-115.
DR PDB; 2WU5; X-ray; 2.80 A; D/H/L=1-115.
DR PDBsum; 1NEK; -.
DR PDBsum; 1NEN; -.
DR PDBsum; 2ACZ; -.
DR PDBsum; 2WDQ; -.
DR PDBsum; 2WDR; -.
DR PDBsum; 2WDV; -.
DR PDBsum; 2WP9; -.
DR PDBsum; 2WS3; -.
DR PDBsum; 2WU2; -.
DR PDBsum; 2WU5; -.
DR AlphaFoldDB; P0AC44; -.
DR SMR; P0AC44; -.
DR BioGRID; 4259943; 25.
DR ComplexPortal; CPX-1931; Respiratory chain complex II.
DR DIP; DIP-10838N; -.
DR IntAct; P0AC44; 1.
DR STRING; 511145.b0722; -.
DR DrugBank; DB07671; 2-[1-METHYLHEXYL]-4,6-DINITROPHENOL.
DR DrugBank; DB04631; Atpenin A5.
DR DrugBank; DB08690; Ubiquinone Q2.
DR jPOST; P0AC44; -.
DR PaxDb; P0AC44; -.
DR PRIDE; P0AC44; -.
DR EnsemblBacteria; AAC73816; AAC73816; b0722.
DR EnsemblBacteria; BAA35389; BAA35389; BAA35389.
DR GeneID; 67413763; -.
DR GeneID; 945322; -.
DR KEGG; ecj:JW0712; -.
DR KEGG; eco:b0722; -.
DR PATRIC; fig|1411691.4.peg.1550; -.
DR EchoBASE; EB0927; -.
DR eggNOG; COG2142; Bacteria.
DR HOGENOM; CLU_151315_2_0_6; -.
DR InParanoid; P0AC44; -.
DR OMA; QWMKVLT; -.
DR PhylomeDB; P0AC44; -.
DR BioCyc; EcoCyc:SDH-MEMB2; -.
DR BioCyc; MetaCyc:SDH-MEMB2; -.
DR UniPathway; UPA00223; -.
DR EvolutionaryTrace; P0AC44; -.
DR PHI-base; PHI:7963; -.
DR PRO; PR:P0AC44; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IMP:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IEP:EcoCyc.
DR GO; GO:0017004; P:cytochrome complex assembly; IMP:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014312; Succ_DH_anchor.
DR PANTHER; PTHR38689; PTHR38689; 1.
DR PIRSF; PIRSF000169; SDH_D; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02968; succ_dehyd_anc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Electron transport; Heme;
KW Iron; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..115
FT /note="Succinate dehydrogenase hydrophobic membrane anchor
FT subunit"
FT /id="PRO_0000158672"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT TOPO_DOM 37..58
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..80
FT /note="Helical"
FT TOPO_DOM 81..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 91..115
FT /note="Helical"
FT BINDING 71
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 83
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000269|PubMed:12560550"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1NEK"
FT HELIX 12..37
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1NEK"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 55..83
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 87..112
FT /evidence="ECO:0007829|PDB:2WDQ"
SQ SEQUENCE 115 AA; 12868 MW; 5CFD0104CB3CC2F9 CRC64;
MVSNASALGR NGVHDFILVR ATAIVLTLYI IYMVGFFATS GELTYEVWIG FFASAFTKVF
TLLALFSILI HAWIGMWQVL TDYVKPLALR LMLQLVIVVA LVVYVIYGFV VVWGV
