FRDA_PROVU
ID FRDA_PROVU Reviewed; 598 AA.
AC P20922;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 118.
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;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3308458; DOI=10.1111/j.1432-1033.1987.tb13362.x;
RA Cole S.T.;
RT "Nucleotide sequence and comparative analysis of the frd operon encoding
RT the fumarate reductase of Proteus vulgaris. Extensive sequence divergence
RT of the membrane anchors and absence of an frd-linked ampC cephalosporinase
RT gene.";
RL Eur. J. Biochem. 167:481-488(1987).
CC -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are
CC responsible for the catalysis of fumarate and succinate
CC interconversion; the fumarate reductase is used in anaerobic growth,
CC and the succinate dehydrogenase is used in aerobic growth.
CC {ECO:0000250|UniProtKB:P00363}.
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; X06144; CAA29501.1; -; Genomic_DNA.
DR PIR; S00107; RDEBFV.
DR AlphaFoldDB; P20922; -.
DR SMR; P20922; -.
DR STRING; 585.DR95_2058; -.
DR eggNOG; COG1053; Bacteria.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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; Transport.
FT CHAIN 1..598
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000158666"
FT REGION 577..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 356..357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 391..397
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 598 AA; 66142 MW; AB205F8CEAA186AD CRC64;
MQTFNADIAI IGAGGAGLRA AIAAAEANPQ LKIALISKVY PMRSHTVAAE GGSAAVTQAH
DSYDFHFNDT VSGGDWLCEQ DVVDYFVEHC PTEMTQLELW GCPWSRKEDG SVNVRRFGGM
KIERTWFAAD KTGFHMLHTL FQTSLKYPQI QRFDEHFVLD ILVDEGHARG VVAINMMEGT
KVQIRANAVI MATGGAGRVY RFNTNGGIVT GDGMGIALRH GVPLRDMEFV QYHPTGLPGS
GILMTEGCRG EGGILVNKDG YRYLQDYGLG PETPLGKPEN KYMELGPRDK VSQAFWHEWR
AGRTIKTHRG DVVHLDLRHL GAKKLHERLP FICELAKAYV GVDPVNEPIP VRPTAHYTMG
GIETNQRTET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEE AVRRAQEATP
ANASALDAQT RDIEDNLKKL MNQKGSENWA QIRDEMGEAM EEGCGIYRTP ELMQKTIDKL
TELKERFKHV EIKDTSSVFN TDLLYKIELG FGLDVAECMA HSAFNRKESR GAHQRLDEGC
TERDDVNFLK HTLAFYNPEG APRLEYSDVK ITKSAPAKRV YGGEATAQDK QNKEKANG
