FRDC_HELPJ
ID FRDC_HELPJ Reviewed; 255 AA.
AC Q9ZMN9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Fumarate reductase cytochrome b subunit;
DE AltName: Full=Quinol-fumarate reductase cytochrome b subunit {ECO:0000305};
DE Short=QFR cytochrome b subunit {ECO:0000305};
GN Name=frdC; OrderedLocusNames=jhp_0179;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: The fumarate reductase enzyme complex is required for
CC fumarate respiration. This subunit anchors the complex in the membrane
CC and binds a diheme cytochrome b. {ECO:0000250|UniProtKB:P17413}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P17413};
CC Note=Binds 2 heme b molecules per subunit, called the proximal (bP) and
CC distal (bD) hemes. {ECO:0000250|UniProtKB:P17413};
CC -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC flavoprotein (frdA), an iron-sulfur protein (frdB), and diheme
CC cytochrome b (frdC). {ECO:0000250|UniProtKB:P17413}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P17413}.
CC -!- SIMILARITY: Belongs to the diheme cytochrome b FrdC family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD05763.1; -; Genomic_DNA.
DR PIR; H71963; H71963.
DR RefSeq; WP_001183641.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZMN9; -.
DR SMR; Q9ZMN9; -.
DR STRING; 85963.jhp_0179; -.
DR EnsemblBacteria; AAD05763; AAD05763; jhp_0179.
DR GeneID; 66521441; -.
DR KEGG; hpj:jhp_0179; -.
DR PATRIC; fig|85963.30.peg.842; -.
DR eggNOG; ENOG5031HUY; Bacteria.
DR OMA; LLAHLHF; -.
DR Proteomes; UP000000804; Chromosome.
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: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:UniProtKB-KW.
DR CDD; cd00581; QFR_TypeB_TM; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR004224; Fum_red_B_TM.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000177; Fumar_rd_cyt_b; 1.
DR SUPFAM; SSF81343; SSF81343; 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..255
FT /note="Fumarate reductase cytochrome b subunit"
FT /id="PRO_0000158684"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bP"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT BINDING 143
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
FT BINDING 182
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="bP"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P17413"
SQ SEQUENCE 255 AA; 28872 MW; E749350188553E50 CRC64;
MQQEEIIEGY YGASKGLKKS GIYAKLDFLQ SATGLILALF MIAHMFLVSS ILISDEAMYK
VAKFFEGSLF LKAGEPAIVS VVAAGVILIL VAHAFLALRK FPINYRQYKV FKTHKHLMKH
GDTSLWFIQA LTGFAMFFLA SIHLFVMLTE PESIGPHGSS YRFVTQNFWL LYIFLLFAVE
LHGSIGLYRL AIKWGWFKNV SIQGLRKIKW AMSVFFIVLG LCTYGAYIKK GLENKDNGIK
TMQEAIEADG KFHKE
