ID   U2PDZ0_LEPWF            Unreviewed;       451 AA.
AC   U2PDZ0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:ERK48740.1};
GN   ORFNames=HMPREF9015_01613 {ECO:0000313|EMBL:ERK48740.1};
OS   Leptotrichia wadei (strain F0279).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=888055 {ECO:0000313|EMBL:ERK48740.1, ECO:0000313|Proteomes:UP000016626};
RN   [1] {ECO:0000313|EMBL:ERK48740.1, ECO:0000313|Proteomes:UP000016626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0279 {ECO:0000313|EMBL:ERK48740.1,
RC   ECO:0000313|Proteomes:UP000016626};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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:ERK48740.1}.
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DR   EMBL; AWVM01000089; ERK48740.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2PDZ0; -.
DR   PATRIC; fig|888055.3.peg.1540; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_1_0_0; -.
DR   Proteomes; UP000016626; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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;
FT   DOMAIN          9..313
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          341..436
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   451 AA;  50298 MW;  D29F51C3A9B00ED0 CRC64;
     MDRKGEIDMK VVVIGCTHAG TAAILNLRKM NPEAEITVFE RNDNISFLSC GIALYVGGVV
     KDPKGLFYSS PEKLKELNVD TKMKHEVKNV DIEGKKIHVV NLENGNEFDE TFDKLIITSG
     SWPIIPPIEG INLNNILLCK NYNHSNEIIE RAKNSQKIVV VGAGYIGVEL VEAFRDNGKE
     VVLVDAEERI LSKYFDKEFT DVAEESFKQR GIVLATGEKV LKFEGSNGNV AKVITDKNEY
     EADMVIMCIG FLPSTSLFKG QLEMLPNGAI KVDEYMRTSN KDVMAAGDCC SVFYNPLQKE
     VYIPLATNAV RMGTLAGINL FENKIKHIGT QGTSGIKIYE NNMAATGLTE ESAKEEGIEV
     ESVIAIDNYR PEFMPTYEKV TLKVIYDKNS RVILGAQLTS KIDLTQSINT LSVCIQNRMT
     IEELAFVDFF FQPHYNKPWN FLNLAGLNAL K
//