ID A0A0R1LVC6_9LACO Unreviewed; 464 AA.
AC A0A0R1LVC6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:KRK97539.1};
GN ORFNames=FD04_GL001568 {ECO:0000313|EMBL:KRK97539.1};
OS Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK97539.1, ECO:0000313|Proteomes:UP000051160};
RN [1] {ECO:0000313|EMBL:KRK97539.1, ECO:0000313|Proteomes:UP000051160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK97539.1,
RC ECO:0000313|Proteomes:UP000051160};
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:KRK97539.1}.
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DR EMBL; AZEE01000029; KRK97539.1; -; Genomic_DNA.
DR RefSeq; WP_056948474.1; NZ_AZEE01000029.1.
DR AlphaFoldDB; A0A0R1LVC6; -.
DR STRING; 1423776.FD04_GL001568; -.
DR PATRIC; fig|1423776.4.peg.1587; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000051160; 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 PRINTS; PR00368; FADPNR.
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 20..443
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 464 AA; 49633 MW; 4298EEF5EBE4A330 CRC64;
MAEKFHFDPT PITQLKKHYD VIVVGSGAAG MTAAIQAHEL GLSPVILEKM DNLGGNTNRA
SSGMNAAETN IQLKHHVVDS YEEFYAETLK GGGNKNNTEL LKYFTEHAAL AIDWLSDHDI
HLDDITITGG MSKMRTHRPS SMAPIGAFLV TELLKQVQKA GIPLFAGLKV TELTTENGRV
TGVKATTGKQ SGPLTADAVV LAAGGFGANQ ELLAKYRPDL EGLKTTNQPG ATGDGIKLAQ
SLGAKLVDMD QVQVHPTVQQ DTPHAYLIGE AVRGEGAILV NKHGDRFVNE LDTRKNVTAA
IDGLNEGGAY LIFDQGIRDR VKAVEFYDHV GLVHTGQSLD ELADQLGFDA ATLKQTVADW
NAAVAGKNDT NFGRSTGMDR DITKAPFFAI HIAPAVHYTM GGIAINHKTE VLKEDGETIN
GLYAAGEIVG GLHGNNRIGG NSIAETVIFG RQAGEQVYNY ISQK
//
