FRDA_HAEIN
ID FRDA_HAEIN Reviewed; 599 AA.
AC P44894;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
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=HI_0835;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:P00363};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + succinate = a menaquinol + fumarate;
CC Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539,
CC ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031; EC=1.3.5.4;
CC Evidence={ECO:0000250|UniProtKB:P00363};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P00363};
CC Note=Binds 1 FAD covalently per subunit.
CC {ECO:0000250|UniProtKB:P00363};
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic
CC anchor proteins (FrdC and FrdD). {ECO:0000250|UniProtKB:P00363}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P00363}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00363}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P00363}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC22493.1; -; Genomic_DNA.
DR PIR; H64097; H64097.
DR RefSeq; NP_438995.1; NC_000907.1.
DR RefSeq; WP_010869064.1; NC_000907.1.
DR AlphaFoldDB; P44894; -.
DR SMR; P44894; -.
DR STRING; 71421.HI_0835; -.
DR PRIDE; P44894; -.
DR EnsemblBacteria; AAC22493; AAC22493; HI_0835.
DR KEGG; hin:HI_0835; -.
DR PATRIC; fig|71421.8.peg.876; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_6; -.
DR OMA; PTAHHFM; -.
DR PhylomeDB; P44894; -.
DR BioCyc; HINF71421:G1GJ1-876-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045284; C:plasma membrane fumarate reductase complex; 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 GO; GO:0006113; P:fermentation; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
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; IPR005884; Fum_red_fp.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR PANTHER; PTHR11632:SF53; PTHR11632:SF53; 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 TIGRFAMs; TIGR01176; fum_red_Fp; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 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; Nucleotide-binding; Oxidoreductase; Reference proteome;
KW Transport.
FT CHAIN 1..599
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000158661"
FT ACT_SITE 233
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT ACT_SITE 249
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 12..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 36..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 44..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 156..158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 212
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 357..358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 381
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 392..398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT MOD_RES 45
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:P00363"
SQ SEQUENCE 599 AA; 65933 MW; 30D4D3B10059236F CRC64;
MQTVNVDIAI VGAGGGGLRA AIAAAEANPN LKIALVSKVY PMRTHTVAAE GGAAAVIKEE
DSYDKHFQDT VAGGDWLCEQ DVVEYFVQHS PVEMTQLERW GCPWSRKADG DVNVRRFGGM
KIERTWFAAD KTGFHLLHTL FQTSIQYPQI QRFDEHFVLD ILVDDGHARG MVAMNMMEGS
LVQINANAVV IATGGGCRAF KFNTNGGIVT GDGLSMAYRH GVPLRDMEFV QYHPTGLPNT
GILMTEGCRG EGGILVNKDG YRYLQDYGLG PETPIGKPQN KYMELGPRDK VSQAFWQEWK
KGNTLKTAKG VDVVHLDLRH LGEKYLHERL PFICELASAY EGVNPVNEPI PVRPVVHYTM
GGIEVDFNSE TRIKGLFAVG ECASSGLHGA NRLGSNSLAE LVVLGRVAGE YAAQRAVEAQ
SVNQSAVDAQ AKDVVARLEA LHKQEGNESW SEIRDEMGTV MEEGCGIYRD QASMQKAVDK
IAELKERYKR IRVSDNSSVF NTDVLYTVEL GYILDVAQSI ANSAIERKES RGAHQRLDYT
ERDDVNYLKH TLAFYNENGA PRIEYSPVKI TKSQPAKRVY GAEAEAQEAA AKAKEQANG
