ID A0A0R1UG07_9LACO Unreviewed; 463 AA.
AC A0A0R1UG07;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Fumarate reductase subunit A {ECO:0000313|EMBL:KRL89506.1};
GN ORFNames=FC46_GL000776 {ECO:0000313|EMBL:KRL89506.1};
OS Lactobacillus kalixensis DSM 16043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423763 {ECO:0000313|EMBL:KRL89506.1, ECO:0000313|Proteomes:UP000051036};
RN [1] {ECO:0000313|EMBL:KRL89506.1, ECO:0000313|Proteomes:UP000051036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16043 {ECO:0000313|EMBL:KRL89506.1,
RC ECO:0000313|Proteomes:UP000051036};
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:KRL89506.1}.
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DR EMBL; AZFM01000022; KRL89506.1; -; Genomic_DNA.
DR RefSeq; WP_057799129.1; NZ_AZFM01000022.1.
DR AlphaFoldDB; A0A0R1UG07; -.
DR STRING; 1423763.FC46_GL000776; -.
DR PATRIC; fig|1423763.3.peg.784; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000051036; 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 19..443
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 463 AA; 49856 MW; 55A3AC94102E6C4F CRC64;
MAKFIFTPNT ADEIADSYDA VIIGAGGTGL TAALQAHELG LKVAVFEKNE QLGGNTTRAS
SGMNASESLV QLQEGIIDNK EDFYKETLKG GGLLNDRDML RYFVDHSAIA IDWLMEHGIE
LTDLTITGGM SKKRAHRPAS MAPVGGYLVT GLLKQIEKEG IHVFNDAKVI KLLQNDEKAI
DGVEVETKAG TKTVHAKAVL LASGGFGASK DIIKKYRPDL VDYKTTNQPG ATGDGLKLAE
AVDAQLMQMN FIQVHPTAQT DTDHTFLIGE GVRGEGAILV NKAGKRFVNE LNTRKIVSNA
ITGLNEDGAY LIFDQGIRDH FKAIEFYDHV GLVEHGATLD ELAETIGVNA ANLNETIAKW
NSEVAQKKDT DFGRTTGMER GIEKGPFFAI HVHPAIHYTM GGIHVTPETE VLDTNGSIID
GLYAAGEVSG GLHGNNRIGG NSIAETVIFG RQAGMQMAKK IRK
//
