ID Q99ZN6_STRP1 Unreviewed; 456 AA.
AC Q99ZN6;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 145.
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:AAK34022.1};
GN OrderedLocusNames=SPy_1150 {ECO:0000313|EMBL:AAK34022.1};
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447 {ECO:0000313|EMBL:AAK34022.1, ECO:0000313|Proteomes:UP000000750};
RN [1] {ECO:0000313|EMBL:AAK34022.1, ECO:0000313|Proteomes:UP000000750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1
RC {ECO:0000313|Proteomes:UP000000750};
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Adjic D., Savic D., Savic G., Lyon K.,
RA Primeaux C., Sezate S.S., Surorov A.N., Kenton S., Lai H., Lin S., Qian Y.,
RA Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
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}.
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DR EMBL; AE004092; AAK34022.1; -; Genomic_DNA.
DR RefSeq; NP_269301.1; NC_002737.2.
DR AlphaFoldDB; Q99ZN6; -.
DR PaxDb; 1314-HKU360_00934; -.
DR KEGG; spy:SPy_1150; -.
DR PATRIC; fig|160490.10.peg.1003; -.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OMA; YSPCAIP; -.
DR Proteomes; UP000000750; Chromosome.
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:AAK34022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000750}.
FT DOMAIN 3..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 347..441
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 456 AA; 49604 MW; 282116EDC8945758 CRC64;
MSKIVVVGAN HAGTACIKTM LTNYGDANEI VVFDQNSNIS FLGCGMALWI GEQIAGPEGL
FYSDKEELES LGAKVYMESP VQSIDYDAKT VTALVDGKNH VETYDKLIFA TGSQPILPPI
KGAEIKEGSL EFEATLENLQ FVKLYQNSAD VIAKLENKDI KRVAVVGAGY IGVELAEAFQ
RKGKEVVLID VVDTCLAGYY DRDLTDLMAK NMEEHGIQLA FGETVKEVAG NGKVEKIITD
KNEYDVDMVI LAVGFRPNTT LGNGKIDLFR NGAFLVNKRQ ETSIPGVYAI GDCATIYDNA
TRDTNYIALA SNAVRTGIVA AHNACGTDLE GIGVQGSNGI SIYGLHMVST GLTLEKAKRL
GFDAAVTEYT DNQKPEFIEH GNFPVTIKIV YDKDSRRILG AQMAAREDVS MGIHMFSLAI
QEGVTIEKLA LTDIFFLPHF NKPYNYITMA ALGAKD
//
