FRDA_HELPY
ID FRDA_HELPY Reviewed; 714 AA.
AC O06913;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 149.
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=HP_0192;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX PubMed=9434188; DOI=10.1016/s0378-1119(97)00550-7;
RA Ge Z., Jiang Q., Kalisiak M.S., Taylor D.E.;
RT "Cloning and functional characterization of Helicobacter pylori fumarate
RT reductase operon comprising three structural genes coding for subunits C, A
RT and B.";
RL Gene 204:227-234(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; U78101; AAC46064.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07259.1; -; Genomic_DNA.
DR PIR; H64543; H64543.
DR RefSeq; NP_206991.1; NC_000915.1.
DR RefSeq; WP_000706021.1; NC_018939.1.
DR AlphaFoldDB; O06913; -.
DR SMR; O06913; -.
DR DIP; DIP-3345N; -.
DR IntAct; O06913; 2.
DR MINT; O06913; -.
DR STRING; 85962.C694_00955; -.
DR PaxDb; O06913; -.
DR EnsemblBacteria; AAD07259; AAD07259; HP_0192.
DR KEGG; hpy:HP_0192; -.
DR PATRIC; fig|85962.47.peg.207; -.
DR eggNOG; COG1053; Bacteria.
DR OMA; DPIPIQP; -.
DR PhylomeDB; O06913; -.
DR BioCyc; MetaCyc:HP0192-MON; -.
DR SABIO-RK; O06913; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
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; Reference proteome; Transport.
FT CHAIN 1..714
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000158662"
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"
FT CONFLICT 112
FT /note="K -> R (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..175
FT /note="HHKVDI -> NTTKWIL (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="K -> E (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="VPA -> MPT (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="R -> K (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 615..624
FT /note="MEISPDFRGY -> WKSALILGAM (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="I -> V (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="E -> D (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="Q -> K (in Ref. 1; AAC46064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 80121 MW; D4639213CB19B3A9 CRC64;
MKITYCDALI IGGGLAGLRA SIACKQKGLN TIVLSLVPVR RSHSAAAQGG MQASLANAKK
SEGDNEDLHF LDTVKGSDWG CDQQVARMFV TTAPKAIREL ASWGVPWTRI KKGDRPAVVN
GEHVTITERD DRHGYILSRD FGGTKKWRTC FTADATGHTM LYAVANEALH HKVDIQDRKD
MLAFIHHDNK CYGAVVRDLI TGEISAYVSK GTLLATGGYG RVYKHTTNAV ICDGAGAASA
LETGVAKLGN MEAVQFHPTA LVPSGILMTE GCRGDGGVLR DKFGRRFMPA YEPEKKELAS
RDVVSRRILE HIQKGYGAKS PYGDHVWLDI AILGRNHVEK NLRDVRDIAM TFAGIDPADS
KEQTKDNMQG VPANEPEYGQ AMAKQKGWIP IKPMQHYSMG GVRTNPKGET HLKGLFCAGE
AACWDLHGFN RLGGNSVSEA VVAGMIIGDY FASHCLEAQI EINTQKVEAF IKESQDYMHF
LLHNEGKEDV YEIRERMKEV MDEKVGVFRE GKRLEEALKE LQELYARSKN ICVKNKVLHN
NPELEDAYRT KKMLKLALCI TQGALLRTES RGAHTRIDYP KRDDEKWLNR TLASWPSAEQ
DMPTIEYEEL DVMKMEISPD FRGYGKKGNF IPHPKKEERD AEILKTILEL EKLGKDRIEV
QHALMPFELQ EKYKARNMRL EDEEVRARGE HLYSFNVHEL LDQHNANLKG EHHE
