DHSD_THEAC
ID DHSD_THEAC Reviewed; 123 AA.
AC Q08717;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN Name=sdhD; OrderedLocusNames=Ta1004;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=8334158; DOI=10.1016/0167-4781(93)90101-i;
RA Bach M., Reilaender H., Gaertner P., Lottspeich F., Michel H.;
RT "Nucleotide sequence of a putative succinate dehydrogenase operon in
RT Thermoplasma acidophilum.";
RL Biochim. Biophys. Acta 1174:103-107(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; X70908; CAA50264.1; -; Genomic_DNA.
DR EMBL; AL445066; CAC12133.1; -; Genomic_DNA.
DR PIR; S34621; S34621.
DR RefSeq; WP_010901415.1; NC_002578.1.
DR AlphaFoldDB; Q08717; -.
DR SMR; Q08717; -.
DR STRING; 273075.Ta1004; -.
DR EnsemblBacteria; CAC12133; CAC12133; CAC12133.
DR GeneID; 1456527; -.
DR KEGG; tac:Ta1004; -.
DR eggNOG; arCOG04162; Archaea.
DR HOGENOM; CLU_2010222_0_0_2; -.
DR OMA; TYHGING; -.
DR OrthoDB; 115843at2157; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000001024; 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:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; 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; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Tricarboxylic acid cycle.
FT CHAIN 1..123
FT /note="Succinate dehydrogenase hydrophobic membrane anchor
FT subunit"
FT /id="PRO_0000158682"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 72
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"
SQ SEQUENCE 123 AA; 13874 MW; 3AECFAEA944EFB07 CRC64;
MAETEKMKYG SLNRFAQAVT GLFLLFFLGV HLYVAHIDFG HPVAFFSSVI NQLHNPWWLA
FFLIFVYIIT YHGINGLNHI VADTSISEKA KRNIGIALMV IYVITIIYGT ILALLVARMT
VPT
