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Database: UniProt
Entry: F0FDG4_STRSA
LinkDB: F0FDG4_STRSA
Original site: F0FDG4_STRSA 
ID   F0FDG4_STRSA            Unreviewed;       458 AA.
AC   F0FDG4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=NADH oxidase {ECO:0000256|ARBA:ARBA00039201};
DE            EC=1.6.3.4 {ECO:0000256|ARBA:ARBA00039092};
GN   Name=nox {ECO:0000313|EMBL:EGC23134.1};
GN   ORFNames=HMPREF9388_0746 {ECO:0000313|EMBL:EGC23134.1};
OS   Streptococcus sanguinis SK353.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888815 {ECO:0000313|EMBL:EGC23134.1, ECO:0000313|Proteomes:UP000004185};
RN   [1] {ECO:0000313|EMBL:EGC23134.1, ECO:0000313|Proteomes:UP000004185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK353 {ECO:0000313|EMBL:EGC23134.1,
RC   ECO:0000313|Proteomes:UP000004185};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+); Xref=Rhea:RHEA:37799,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036014};
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:EGC23134.1}.
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DR   EMBL; AEWY01000003; EGC23134.1; -; Genomic_DNA.
DR   RefSeq; WP_002897609.1; NZ_GL872307.1.
DR   AlphaFoldDB; F0FDG4; -.
DR   PATRIC; fig|888815.3.peg.730; -.
DR   HOGENOM; CLU_003291_1_0_9; -.
DR   Proteomes; UP000004185; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW   Oxidoreductase {ECO:0000313|EMBL:EGC23134.1}.
FT   DOMAIN          3..319
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          346..444
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   458 AA;  50368 MW;  8EB2BECD79150A84 CRC64;
     MSKIVVVGAN HAGTACINTM LDNYGAENEV VIFDQNSNIS FLACGMALWI GQQISKPDGL
     FYADKETFEA KGAKVYMNSP VESIDYDAKK VTAIVDGKEH VESYDKLILA TGSQPILPPI
     KGAEMDPNSR EFKSTLENLQ FVKLYQNAAD VIEKLQDKSK HIERVAVVGA GYIGVELAEA
     FKRLGKEVIL IDVVDTCLAG YYDHDLSEMM RQNLEDNGVQ LAFGQTVQAI EGENKVERIV
     TDKASYDVDM VVLAVGFRPN TGLGAGKLET FRNGAFLVDK KQETSIKDVY AIGDCATVYD
     NSINDTNYIA LASNALRSGI VAAHNACGHE LESNGVQGSN GIEIFGLKMV STGLTEEKAK
     RFGYSPAVVE FKDTQKPTFL EKVEHHDVTI KIVYDKDTRV VLGAQMVSRE DMSMGIHMFS
     LAIQEKVTID KLALLDLFFL PHFNKPYNYI TQAALKAK
//
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