ID Q9CP56_PASMU Unreviewed; 599 AA.
AC Q9CP56;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 135.
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:AAK02285.1};
GN OrderedLocusNames=PM0201 {ECO:0000313|EMBL:AAK02285.1};
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK02285.1, ECO:0000313|Proteomes:UP000000809};
RN [1] {ECO:0000313|EMBL:AAK02285.1, ECO:0000313|Proteomes:UP000000809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK02285.1,
RC ECO:0000313|Proteomes:UP000000809};
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR EMBL; AE004439; AAK02285.1; -; Genomic_DNA.
DR RefSeq; WP_005723450.1; NC_002663.1.
DR AlphaFoldDB; Q9CP56; -.
DR STRING; 272843.PM0201; -.
DR EnsemblBacteria; AAK02285; AAK02285; PM0201.
DR GeneID; 77207549; -.
DR KEGG; pmu:PM0201; -.
DR HOGENOM; CLU_014312_6_2_6; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000000809; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000809};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362050}.
FT DOMAIN 7..398
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 454..580
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 467..494
FT /evidence="ECO:0000256|SAM:Coils"
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 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 381
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 397..398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ SEQUENCE 599 AA; 66175 MW; E8E644B758BDFFC2 CRC64;
MQTVNVDIAI VGAGGGGLRA AIAAAEANPN LKIALVSKVY PMRSHTVAAE GGAAAVIKEE
DSYDKHFHDT VAGGDWLCEQ DVVEYFVQHS PVEMTQLERW GCPWSRKQDG DVNVRRFGGM
KIERTWFAAD KTGFHLLHTL FQTSIQYPQI VRFDEHFVLD ILVDDGHARG MVAMNMMEGT
LVQINANAVV IATGGGCRAF RFNTNGGIVT GDGLSMAYRH GVPLRDMEFV QYHPTGLPNT
GILMTEGCRG EGGILVNKDG YRYLQDYGLG PETPIGKPEN KYMELGPRDK VSQAFWQELQ
KGNTLKTAKG VDVVHLDLRH LGEKYLHERL PFICELAQAY EGVDPAKAPI PVRPVVHYTM
GGIEVDFNSE TRIKGLFAVG ECASSGLHGA NRLGSNSLAE LVVLGRVAGE YAAQRAVEAP
AVNQTAVDAQ ARDIVQRLED LYHQEGNESW SEIRDEMGDA MEEGCGIYRT QESMQKAVDK
IAELKERYKR IRITDRSSVF NTNVLYTVEL GYILDVAQSI ANSAIERKES RGAHQRLDYT
ERDDVNYLKH TLAFYNGDDA PRIEYSDVKI TKSQPAKRVY GAEAEAQEAA KANKENANG
//
