ID   DHSD_PARDE              Reviewed;         129 AA.
AC   Q59660;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN   Name=sdhD;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RA   Dickins M.A., Dhawan T., Gunsalus R.P., Schroeder I., Cecchini G.;
RT   "Cloning, sequencing, and expression of the succinate-ubiquinone
RT   oxidoreductase (SdhCDAB) operon from Paracoccus denitrificans.";
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
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 inner membrane; Multi-pass membrane protein.
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; U31902; AAA75176.1; -; Genomic_DNA.
DR   PIR; T46879; T46879.
DR   RefSeq; WP_011746913.1; NZ_FOYK01000010.1.
DR   AlphaFoldDB; Q59660; -.
DR   SMR; Q59660; -.
DR   OMA; YFARPFP; -.
DR   UniPathway; UPA00223; -.
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   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   Pfam; PF01127; Sdh_cyt; 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; Transmembrane; Transmembrane helix; Transport;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..129
FT                   /note="Succinate dehydrogenase hydrophobic membrane anchor
FT                   subunit"
FT                   /id="PRO_0000158676"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        44..65
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        88..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        98..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
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         90
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   129 AA;  13934 MW;  249BC7EE20C954B4 CRC64;
     MRYITPRKAA EGLGSAHEGT QHHWAMTVSA VALTVLTPLF MIVVARAIGL SQEQLLAYFG
     RPFPALITAL FVIVGMVHFI KGTRIMIDDY FQGGTRKAAI IFSVIFGWAV IAAAVYALAR
     MGLGAIVVL