FRDA_SERS3
ID FRDA_SERS3 Reviewed; 598 AA.
AC V3TQ67;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
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 {ECO:0000303|PubMed:24374335}; ORFNames=Ser39006_04053;
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; unclassified Serratia.
OX NCBI_TaxID=104623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=24336377; DOI=10.1128/genomea.01039-13;
RA Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA Brugger K., Brown S.D., Salmond G.P.;
RT "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT for analysis of the biosynthesis and regulation of prodigiosin, a
RT carbapenem, and gas vesicles.";
RL Genome Announc. 1:E01039-E01039(2013).
RN [2]
RP FUNCTION, COFACTOR, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=24374335; DOI=10.1016/j.febslet.2013.12.019;
RA McNeil M.B., Hampton H.G., Hards K.J., Watson B.N., Cook G.M.,
RA Fineran P.C.;
RT "The succinate dehydrogenase assembly factor, SdhE, is required for the
RT flavinylation and activation of fumarate reductase in bacteria.";
RL FEBS Lett. 588:414-421(2014).
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, ECO:0000305|PubMed:24374335}.
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:0000269|PubMed:24374335};
CC Note=Flavinylated by SdhE, flavinylation occurs at a low level in the
CC absence of SdhE. {ECO:0000269|PubMed:24374335};
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) (By similarity). Interacts with SdhE
CC (PubMed:24374335). {ECO:0000250|UniProtKB:P00363,
CC ECO:0000269|PubMed:24374335}.
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 -!- DISRUPTION PHENOTYPE: Significant growth defect during anaerobic growth
CC on glycerol fumarate medium (a quadruple fdrABCD deletion); the defect
CC is similar in strains also containing an sdhE deletion
CC (PubMed:24374335). {ECO:0000269|PubMed:24374335}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily.
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DR EMBL; CP025084; ESN61646.1; -; Genomic_DNA.
DR RefSeq; WP_021017313.1; NZ_CP025085.1.
DR AlphaFoldDB; V3TQ67; -.
DR SMR; V3TQ67; -.
DR IntAct; V3TQ67; 1.
DR MINT; V3TQ67; -.
DR STRING; 104623.Ser39006_04053; -.
DR eggNOG; COG1053; Bacteria.
DR OrthoDB; 153138at2; -.
DR Proteomes; UP000017700; Chromosome.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Membrane; Nucleotide-binding; Oxidoreductase; Reference proteome;
KW Transport.
FT CHAIN 1..598
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000438886"
FT REGION 577..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Basic and acidic residues"
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; 66097 MW; BED130B2231AAC6A CRC64;
MQTFNADLAI IGAGGAGLRA AIAAAEANPQ LKIALISKVY PMRSHTVAAE GGSAAVTQDH
DSFDFHFHDT VAGGDWLCEQ DVVDQFVQSC PREMTQLEQW GCPWSRKPDG SVNVRRFGGM
KIERTWFAAD KTGFHMLHTL FQTSLKYPQI QRFDEHFVLD ILVDDGQARG LVAINMMEGT
LVQIRANAVI MATGGAGRVY RYNTNGGIVT GDGMGMAFRH GVPLRDMEFV QYHPTGLPGS
GILMTEGCRG EGGIMVNKDG YRYLQDYGMG PETPLGQPKN KYMELGPRDK VSQAFWHEWR
AGRTISTPLG DVVYLDLRHL GEKKLKERLP FICELAQAYV GVDPVKEPIP IRPTAHYTMG
GIETDQQCET RIKGLFAAGE CSSVGLHGAN RLGSNSLAEL VVFGRIAGEH ATQRSLESAP
ANASALDAQA RDVEQRLHTL MKQEGTESWA KIRDEMGISM EEGCGIYRTT ELMQKTLDKL
AELKERFKRV KITDHSSVFN TDLLYTIELG HSLDVAQCMA HSAINRKESR GAHQRLDEGC
TERDDVNFLK HTLAFYNPEG APRLEYSDVK ITKLPPAKRV YGGEADAQEK SDKEQANG
