ID A0A060B860_9GAMM Unreviewed; 129 AA.
AC A0A060B860;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit {ECO:0000256|ARBA:ARBA00020076};
GN Name=sdhC {ECO:0000313|EMBL:HCA01445.1};
GN ORFNames=DEO68_04485 {ECO:0000313|EMBL:HCA01445.1};
OS Halomonas campaniensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=213554 {ECO:0000313|EMBL:HCA01445.1, ECO:0000313|Proteomes:UP000262828};
RN [1] {ECO:0000313|EMBL:HCA01445.1, ECO:0000313|Proteomes:UP000262828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBA11284 {ECO:0000313|EMBL:HCA01445.1};
RX PubMed=30148503; DOI=.1038/nbt.4229;
RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A.,
RA Chaumeil P.A., Hugenholtz P.;
RT "A standardized bacterial taxonomy based on genome phylogeny substantially
RT revises the tree of life.";
RL Nat. Biotechnol. 36:996-1004(2018).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000256|ARBA:ARBA00004050}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000178-1};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000256|PIRSR:PIRSR000178-1};
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.
CC {ECO:0000256|ARBA:ARBA00025912}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family.
CC {ECO:0000256|ARBA:ARBA00007244}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:HCA01445.1}.
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DR EMBL; DOTR01000022; HCA01445.1; -; Genomic_DNA.
DR KEGG; hcs:FF32_11165; -.
DR HOGENOM; CLU_094691_2_1_6; -.
DR OrthoDB; 9799441at2; -.
DR Proteomes; UP000262828; Unassembled WGS sequence.
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:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd03499; SQR_TypeC_SdhC; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 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 NCBIfam; TIGR02970; succ_dehyd_cytB; 1.
DR PANTHER; PTHR10978; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT; 1.
DR PANTHER; PTHR10978:SF5; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT, MITOCHONDRIAL; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR PROSITE; PS01000; SDH_CYT_1; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000178-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000178-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000178-1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT BINDING 85
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:0000256|PIRSR:PIRSR000178-1"
SQ SEQUENCE 129 AA; 13848 MW; C81F5FB4A24491E0 CRC64;
MYNAVNSKRP VNLDLTTIHF PLPALTSITH RITGVILFVG LIFAFWALGK SLSSPAGFDA
VSNALANNFF AKFIAWGLLS ALAFHFVAGI KHLLMDADIG VTLEGGVKKA QITVVVSVVL
IILAGVWVW
//
