ID A0A1F8T7F7_9CHLR Unreviewed; 115 AA.
AC A0A1F8T7F7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Succinate dehydrogenase, cytochrome b556 subunit {ECO:0000313|EMBL:OGO68085.1};
GN ORFNames=A2Z37_12450 {ECO:0000313|EMBL:OGO68085.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_62_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797671 {ECO:0000313|EMBL:OGO68085.1, ECO:0000313|Proteomes:UP000176680};
RN [1] {ECO:0000313|EMBL:OGO68085.1, ECO:0000313|Proteomes:UP000176680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGO68085.1}.
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DR EMBL; MGOM01000115; OGO68085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8T7F7; -.
DR Proteomes; UP000176680; 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 Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR039023; SdhC_prok.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR NCBIfam; TIGR02970; succ_dehyd_cytB; 1.
DR PANTHER; PTHR41910; SUCCINATE DEHYDROGENASE 2 MEMBRANE SUBUNIT SDHC; 1.
DR PANTHER; PTHR41910:SF1; SUCCINATE DEHYDROGENASE 2 MEMBRANE SUBUNIT SDHC; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000178-1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 67
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 115 AA; 12655 MW; 8E1F8167D20284C5 CRC64;
MYRSTGFVSF VLRRLTGIAL VLYLIAHIWV IGSVNGGTEL FNSRLAAVQT PIFKLAEVAL
LAAVVYHAFD GVRLLIVHYF DVTEYRKSLF YAAFVVSAIL TIAGGLPILL FAFQG
//
