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
//