ID   DHSC_PARDE              Reviewed;         130 AA.
AC   Q59659;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Succinate dehydrogenase cytochrome b556 subunit;
DE            Short=Cytochrome b-556;
GN   Name=sdhC;
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. The complex can form homotrimers (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR   EMBL; U31902; AAA75175.1; -; Genomic_DNA.
DR   PIR; T46878; T46878.
DR   RefSeq; WP_011746912.1; NZ_PPGA01000002.1.
DR   AlphaFoldDB; Q59659; -.
DR   SMR; Q59659; -.
DR   OMA; YHLVAGI; -.
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: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; IPR018495; Succ_DH_cyt_bsu_CS.
DR   InterPro; IPR014314; Succ_DH_cytb556.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   PANTHER; PTHR10978; PTHR10978; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
DR   TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
DR   PROSITE; PS01001; SDH_CYT_2; 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..130
FT                   /note="Succinate dehydrogenase cytochrome b556 subunit"
FT                   /id="PRO_0000203512"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        27..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        53..68
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        90..109
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
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   130 AA;  14277 MW;  3518FE59FE1CCA56 CRC64;
     MADVNRGNRP LSPHLQVYRL PLAAITSIMT RITGHALVAG IVLITWWLVA AVTSPGAFAC
     ADWVVRSWLG FIILTGSMWA LWYHLLAGLR HLFYDAGYGL EIEQAHKSSQ ALIAGSVVLA
     VLTLIVFFVF