ID   C560_CYACA              Reviewed;         132 AA.
AC   P48935;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Succinate dehydrogenase cytochrome b560 subunit;
DE   AltName: Full=Succinate dehydrogenase, subunit III;
GN   Name=SDH3; Synonyms=SDHC;
OS   Cyanidium caldarium (Red alga).
OG   Mitochondrion.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=8821668; DOI=10.1007/bf02221585;
RA   Viehmann S., Richard O., Boyen C., Zetsche K.;
RT   "Genes for two subunits of succinate dehydrogenase form a cluster on the
RT   mitochondrial genome of Rhodophyta.";
RL   Curr. Genet. 29:199-201(1996).
CC   -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). {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: Forms part of complex II containing four subunits: a 70 kDa
CC       flavoprotein (FP), a 27 kDa iron-sulfur protein (IP), a cytochrome B
CC       and a membrane-anchoring protein.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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; Z48930; CAA88765.1; -; Genomic_DNA.
DR   PIR; S62755; S62755.
DR   AlphaFoldDB; P48935; -.
DR   SMR; P48935; -.
DR   UniPathway; UPA00223; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner 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; PS01000; SDH_CYT_1; 1.
DR   PROSITE; PS01001; SDH_CYT_2; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Transmembrane; Transmembrane helix;
KW   Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..132
FT                   /note="Succinate dehydrogenase cytochrome b560 subunit"
FT                   /id="PRO_0000203518"
FT   TRANSMEM        32..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         86
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   132 AA;  15979 MW;  2CA3E86079DEC3FD CRC64;
     MFYKNRPLSP YVTIYSSQWT SISSIFHRLS GLYLVFFLFV LFCSIKFLFC FSTFWFVYKF
     VKTCFFFILS FFIVFIVFSM YSLFYHFFIG LRHLVWDEVI LMEDNFVTMS TKLSLSLSLV
     LVLINCLRYF LV