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Database: UniProt
Entry: A0A085G2K3_9GAMM
LinkDB: A0A085G2K3_9GAMM
Original site: A0A085G2K3_9GAMM 
ID   A0A085G2K3_9GAMM        Unreviewed;       553 AA.
AC   A0A085G2K3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Fumarate reductase flavoprotein subunit {ECO:0000256|RuleBase:RU362050};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362050};
GN   Name=frdA {ECO:0000313|EMBL:KFC77948.1};
GN   ORFNames=GEAM_3971 {ECO:0000313|EMBL:KFC77948.1};
OS   Ewingella americana ATCC 33852.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Ewingella.
OX   NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC77948.1, ECO:0000313|Proteomes:UP000028640};
RN   [1] {ECO:0000313|EMBL:KFC77948.1, ECO:0000313|Proteomes:UP000028640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC77948.1,
RC   ECO:0000313|Proteomes:UP000028640};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362050};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         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   -!- 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:KFC77948.1}.
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DR   EMBL; JMPJ01000071; KFC77948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085G2K3; -.
DR   STRING; 910964.GEAM_3971; -.
DR   eggNOG; COG1053; Bacteria.
DR   Proteomes; UP000028640; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:UniProtKB-UniRule.
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; 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   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.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU362050};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362050};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362050}; 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:UP000028640};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362050}.
FT   DOMAIN          2..351
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          408..536
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          532..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        242
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   553 AA;  61535 MW;  B933D7FFBBA0A1BC CRC64;
     MAAEGGSAAV TQDHDSFAYH FQDTVSGGDW LCEQDVVDHF VHQCPEEMAQ LEIWGCPWSR
     KDDGSINVRR FGGMKIERTW FAADKTGFHI LHTLFQTSLK YPKIKRFDEH FVLDILVDDG
     RVHGVVAINM MEGEKVQIRA NAVVMATGGA GRVYRYNTNG GIVTGDGMGM ALRHGIPLRD
     MEFVQYHPTG LPGSGILMTE GCRGEGGILI NKEGYRYLQD YGMGPETPLG EPKNKYMELG
     PRDKVSQAFW HEWRAGRTES TPRGDVVYLD LRHLGEKKLR ERLPFICELA KAYVGVDPVN
     EPIPVRPTAH YTMGGIETNA QCETRIKGLF AVGECSSVGL HGANRLGSNS LAELVVFGRM
     AGEQAALRAT ETVSTANSAA LDAQVADIEN RLQALMAQEG DESWATIRDE MGMSMEEGCG
     IYRTPELMQK TIDKLAELKQ RYKRIKIKDT SSVFNTDLLY TLELGYGLDV AECMAHSAFH
     RKESRGAHQR LDEGCTQRDD ENFLKHTLAF YQPDAAPRLE YGDVKITTLP PAKRVYGGES
     DAQDKKDKEQ SHG
//
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