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Database: UniProt
Entry: A0A0R1UX23_9LACO
LinkDB: A0A0R1UX23_9LACO
Original site: A0A0R1UX23_9LACO 
ID   A0A0R1UX23_9LACO        Unreviewed;       476 AA.
AC   A0A0R1UX23;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:KRL97808.1};
GN   ORFNames=FD50_GL001178 {ECO:0000313|EMBL:KRL97808.1};
OS   Liquorilactobacillus satsumensis DSM 16230 = JCM 12392.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL97808.1, ECO:0000313|Proteomes:UP000051166};
RN   [1] {ECO:0000313|EMBL:KRL97808.1, ECO:0000313|Proteomes:UP000051166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL97808.1,
RC   ECO:0000313|Proteomes:UP000051166};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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:KRL97808.1}.
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DR   EMBL; AZFQ01000049; KRL97808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1UX23; -.
DR   STRING; 1423801.FD50_GL001178; -.
DR   PATRIC; fig|1423801.4.peg.1201; -.
DR   Proteomes; UP000051166; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; IPR010960; Flavocytochrome_c.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU366062};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU366062};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366062}.
FT   DOMAIN          31..455
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   476 AA;  50833 MW;  74FA810637DB0F68 CRC64;
     MVASTNILGG KIVGAFSFST TAPEKLQDKY DVVIVGSGAT GLTCALQAHE LGLQPLVVEK
     MAKIGGNTNR ASSGMNAAET NVQLQHGIVD SFAEFYQETY HGGGYLNDPQ LLRYFSTHAV
     LALDWLSAHG IELSDLTLTG GMSKKRAHRP ASTAPIGAFL IQGLLQALQQ QKIPLVTETT
     VTRLLRSTSG ATQGVEVKFA DGTKKTLHSK VVVLATGGFG ASKELLQKYR PDLLGYRTTN
     HAGATGDGLR LAHQVGAELM QMNLIQVHPT VQQDNPHAFL IGEAVRGEGA LLVSKGKRFV
     NELDTRRIVS NQITALPEKS AYLVFDQQVR ERVKAIDFYL KIGLVVTASS IAELAQKVGF
     EVAKLEETVK TWNQAVERGL DPQFGRTTGF GNGLTTAPYY AIHVAPAVHY TMGGIHINEK
     TQVLDGNGDV IPGLLAAGEV AGGLHGNNRI GGNSIAETIV FGRQAGQQAK VFTEQG
//
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