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Database: UniProt
Entry: G0M2U8_LACPE
LinkDB: G0M2U8_LACPE
Original site: G0M2U8_LACPE 
ID   G0M2U8_LACPE            Unreviewed;       452 AA.
AC   G0M2U8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:CCC16411.1};
DE            EC=1.6.-.- {ECO:0000313|EMBL:CCC16411.1};
GN   ORFNames=LPENT_01107 {ECO:0000313|EMBL:CCC16411.1};
OS   Lactiplantibacillus pentosus IG1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC16411.1};
RN   [1] {ECO:0000313|EMBL:CCC16411.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IG1 {ECO:0000313|EMBL:CCC16411.1};
RA   Maldonado-Barragan A., Caballero-Guerrero B., Lucena-Padros H.,
RA   Ruiz-Barba J.L.;
RT   "Genome Sequence of Lactobacillus pentosus IG1, a Strain Isolated from
RT   Spanish-Style Green Olive Fermentations.";
RL   J. Bacteriol. 193:5605-5605(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR   EMBL; FR874854; CCC16411.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0M2U8; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43429:SF1; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW   Oxidoreductase {ECO:0000313|EMBL:CCC16411.1}.
FT   DOMAIN          1..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          332..431
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   452 AA;  49324 MW;  6B8BA6B15A3F3B90 CRC64;
     MKVAIIGCTH AGIAAMRQIL KYYPGTEITV YERHATISYM SCGTYLHLGG TIKDLDQALY
     ANPDEFSKQG VQMRMQHDVI KVDATKHTIL AQNLQTKTME TDHYDKLVMA TGSLTAIPAI
     PGVENPKVML CKTCEQAQQL YEAAQHAKQI AIVGGGYAGV ELAEGYIKSG HAVTLYQRGP
     QLIDEYLDAK LANKVEALLT SHGIDVRTNA QVTGFQDTPD NRLQVTTADS ETIYDMAVIC
     PGVIPQSELL AGQVNRTKQG AIVTDRYMGT SNSDIFAAGD VTEVKFNPTK DHAYMPLVSH
     AIRQGALAGI NIFDKRLGSI GTQATTGMLI FGQTIACTGM TLTAAKAAHF EAKTAVYEGN
     YRPDFMPTTA KITIELVYDQ QTRKVLGAQL MSAHEVSQSA NTLSVIIHNG NTIDELAFMD
     MLFSPNFDEP FNYLNLAAQA AVDQEHGYRR NN
//
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