ID A0A091CEG1_9ENTE Unreviewed; 443 AA.
AC A0A091CEG1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:KFN92968.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KFN92968.1};
GN ORFNames=TMU3MR103_0219 {ECO:0000313|EMBL:KFN92968.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN92968.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN92968.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN92968.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFN92968.1}.
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DR EMBL; JPVT01000020; KFN92968.1; -; Genomic_DNA.
DR RefSeq; WP_038021889.1; NZ_JPVT01000020.1.
DR AlphaFoldDB; A0A091CEG1; -.
DR PATRIC; fig|1302648.3.peg.205; -.
DR Proteomes; UP000029381; Unassembled WGS sequence.
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; COENZYME A DISULFIDE REDUCTASE; 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:KFN92968.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029381}.
FT DOMAIN 3..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 443 AA; 49103 MW; 040D9D04C79FC283 CRC64;
MTKTVIIGTN HAGLAAANAI LDNSEQEVVM IERNENFSYL SCGTALWVGQ QIDSVDGLFY
TNREDFEAKG AKVRTQTNVD NIDFEAKIVY ATTSQGENVT EDYDKLVLAT GSIPISPKVP
GRELENITFM KHYEEGQKID QLFEHKDIEN VAVIGAGYIG VEMAEAAKRR DKNVLLFDAL
DRSLPSYYDA WFTDDMDKNL ANHGIELHYG ELVKEYKGTN KVEQIVTEKG EYEVDLVINA
IGFLPNNQLA KDHLELFTNG AYLVDRHQQT SDPDVYAVGD CATVYSNALQ ATTYIALASN
ALRTGMVAGE NIVGNAVESP GVQGSNGISI FGYHMVSTGY SVESAAKFDL NVKYTDIEDT
QKPEFMKEND NVKLRIVYEA TSRRIVGAQM SSTTSDISMA IHMFSLAIEH QVTVDELGKL
DLFFLPHFNQ PYNYINKAAL AAE
//
