DHSD_SHIFL
ID DHSD_SHIFL Reviewed; 115 AA.
AC P0AC46; P10445;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN Name=sdhD; OrderedLocusNames=SF0575, S0588;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000250};
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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; AE005674; AAN42219.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16092.1; -; Genomic_DNA.
DR RefSeq; NP_706512.1; NC_004337.2.
DR RefSeq; WP_000254365.1; NZ_WPGW01000035.1.
DR AlphaFoldDB; P0AC46; -.
DR SMR; P0AC46; -.
DR STRING; 198214.SF0575; -.
DR EnsemblBacteria; AAN42219; AAN42219; SF0575.
DR EnsemblBacteria; AAP16092; AAP16092; S0588.
DR GeneID; 1023493; -.
DR GeneID; 67413763; -.
DR KEGG; sfl:SF0575; -.
DR KEGG; sfx:S0588; -.
DR PATRIC; fig|198214.7.peg.666; -.
DR HOGENOM; CLU_151315_2_0_6; -.
DR OMA; QWMKVLT; -.
DR OrthoDB; 2048140at2; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW 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_0000158675"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..58
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 81..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..115
FT /note="Helical"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
SQ SEQUENCE 115 AA; 12868 MW; 5CFD0104CB3CC2F9 CRC64;
MVSNASALGR NGVHDFILVR ATAIVLTLYI IYMVGFFATS GELTYEVWIG FFASAFTKVF
TLLALFSILI HAWIGMWQVL TDYVKPLALR LMLQLVIVVA LVVYVIYGFV VVWGV
