ID A0A084A327_9GAMM Unreviewed; 598 AA.
AC A0A084A327;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Fumarate reductase flavoprotein subunit {ECO:0000256|ARBA:ARBA00014044, ECO:0000256|RuleBase:RU362050};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362050};
GN Name=frdA {ECO:0000313|EMBL:KEY59706.1};
GN ORFNames=SRDD_12820 {ECO:0000313|EMBL:KEY59706.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY59706.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY59706.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY59706.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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=1.3.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034412};
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=1.3.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000030,
CC ECO:0000256|RuleBase:RU362050};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR630664-51, ECO:0000256|RuleBase:RU362050};
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:0000256|RuleBase:RU362050}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004515}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004515}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004515}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC ECO:0000256|RuleBase:RU362050}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEY59706.1}.
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DR EMBL; AYKS02000041; KEY59706.1; -; Genomic_DNA.
DR RefSeq; WP_023489439.1; NZ_AYKS02000041.1.
DR AlphaFoldDB; A0A084A327; -.
DR STRING; 1410619.SRDD_12820; -.
DR eggNOG; COG1053; Bacteria.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000017810; Unassembled WGS sequence.
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:RHEA.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01176; fum_red_Fp; 1.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632:SF82; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU362050};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR630664-51};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW 51}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362050};
KW Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362050}.
FT DOMAIN 7..397
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 453..581
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT BINDING 12..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 37..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 212
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 396..397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ SEQUENCE 598 AA; 66053 MW; 92FD200E8F5FC6C1 CRC64;
MQTFNADLAI IGAGGAGLRA AIAAAEANPQ IKIALISKVY PMRSHTVAAE GGSAAVTQPH
DSFDYHFQDT VAGGDWLCEQ DVVDHFVHSC PQEMTQLELW GCPWSRKPDG SVNVRRFGGM
KIERTWFAAD KTGFHMLHTL FQTSLKYPQI QRFDEHFVLD VLVDDGQARG VVALNMMEGT
RVLIRSNAVI LATGGAGRVY RYNTNGGIVT GDGMGMAFHH GVPLRDMEFV QYHPTGLPGS
GILMTEGCRG EGGILVNKDG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR
AGRTIPTPRG DVVYLDLRHL GEKKLLERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG
GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRVAGEN AARRALEAPP
ANDSALDAQG RDVETRLSNL MKQEGNENWA KIRDEMGLSM EEGCGIYRTP ELMQKTVDKL
AELKERFKRV KITDSTNVFN TDLLYTIELG HGLDVAECMA HSALNRRESR GAHQRLDEGC
TERDDVNFLK HTLTFHNPDG APRLEYSDVK ITKLPPAKRV YGAEAEAQEK KDKEQANG
//
