FRDA_HELPJ
ID FRDA_HELPJ Reviewed; 714 AA.
AC Q9ZMP0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
DE AltName: Full=Quinol-fumarate reductase flavoprotein subunit {ECO:0000305};
DE Short=QFR flavoprotein subunit {ECO:0000305};
GN Name=frdA; OrderedLocusNames=jhp_0178;
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. {ECO:0000250|UniProtKB:P17412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4;
CC Evidence={ECO:0000250|UniProtKB:P17412};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P17412};
CC Note=Binds 1 FAD covalently per subunit.
CC {ECO:0000250|UniProtKB:P17412};
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:P17412}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P17412}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P17412}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P17412}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; AE001439; AAD05762.1; -; Genomic_DNA.
DR PIR; G71963; G71963.
DR RefSeq; WP_000705948.1; NC_000921.1.
DR AlphaFoldDB; Q9ZMP0; -.
DR SMR; Q9ZMP0; -.
DR IntAct; Q9ZMP0; 1.
DR STRING; 85963.jhp_0178; -.
DR EnsemblBacteria; AAD05762; AAD05762; jhp_0178.
DR KEGG; hpj:jhp_0178; -.
DR eggNOG; COG1053; Bacteria.
DR OMA; DPIPIQP; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 2.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Transport.
FT CHAIN 1..714
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000158663"
FT ACT_SITE 257
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT ACT_SITE 273
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 13..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17412"
FT BINDING 42..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17412"
FT BINDING 49..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17412"
FT BINDING 420
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17412"
FT BINDING 436..437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17412"
FT MOD_RES 43
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:P17412"
SQ SEQUENCE 714 AA; 80120 MW; CE6F1041EDAEC977 CRC64;
MKITYCDALI IGGGLAGLRA SIACKQKGLN TIVLSLVPVR RSHSAAAQGG MQASLANAKK
SEGDNEDLHF LDTVKGSDWG CDQQVARMFV TTAPKAIREL ASWGVPWTRI KKGDRPAVVN
GEHVIITERD DRHGYILSRD FGGTKKWRTC FTADATGHTM LYAVANEALH HKVDIQDRKD
MLAFIHHDNK CYGAVVRDLI TGEISAYVSK GTLLATGGYG RVYKHTTNAV ICDGAGAASA
LETGVAKLGN MEAVQFHPTA LVPSGILMTE GCRGDGGVLR DKFGRRFMPA YEPEKKELAS
RDVVSRRILE HIQKGYGAKS PYGDHVWLDI AILGRNHVEK NLRDVRDIAM TFAGIDPADS
EEQTKDNMQG APTNEPEYGQ AMAKQKGWIP IKPMQHYSMG GVRTNPKGET HLKGLFCAGE
AACWDLHGFN RLGGNSVSEP VVAGMIIGDY FASHCLEAQI EINTQKVEAF IKESQDYMHF
LLHNEGKEDV YEIRERMKEV MDEKVGVFRE GKKLEEALKE LQELYARSKN ICVKNKVLHN
NPELEDAYRT KKMLKLALCI TQGALLRTES RGAHTRIDYP KRDDEKWLNR TLASWPSAEQ
DMPTIEYEEL DVMKMEISPD FRGYGKKGNF IPHPKKEERD AEILKTILEL EKLGKDRIEV
QHALMPFELQ EKYKARNMRL EDEEVRARGE HLYSFNVHDL LDQHNANLKG EHHE
