ID   NOSO_STAAR              Reviewed;         358 AA.
AC   Q6GFE2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Nitric oxide synthase oxygenase;
DE            EC=1.14.14.47 {ECO:0000250|UniProtKB:O34453};
DE   AltName: Full=NOSoxy-like protein;
DE   AltName: Full=SANOS;
GN   Name=nos; OrderedLocusNames=SAR2007;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the production of nitric oxide. {ECO:0000250,
CC       ECO:0000250|UniProtKB:O34453}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-arginine + 4 O2 + 3 reduced [flavodoxin] = 5 H(+) + 4 H2O
CC         + 2 L-citrulline + 2 nitric oxide + 3 oxidized [flavodoxin];
CC         Xref=Rhea:RHEA:52324, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57743, ChEBI:CHEBI:58210; EC=1.14.14.47;
CC         Evidence={ECO:0000250|UniProtKB:O34453};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:O34453};
CC   -!- COFACTOR:
CC       Name=(6S)-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:57453;
CC         Evidence={ECO:0000250|UniProtKB:O34453};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O34453}.
CC   -!- MISCELLANEOUS: This protein is similar to the oxygenase domain of
CC       eukaryotic nitric oxide synthases but lacks the reductase domain which,
CC       in eukaryotes, is responsible for transfer of electrons to the ferric
CC       heme during nitric oxide synthesis.
CC   -!- SIMILARITY: Belongs to the NOS family. Bacterial NOS oxygenase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BX571856; CAG40992.1; -; Genomic_DNA.
DR   RefSeq; WP_000897633.1; NC_002952.2.
DR   AlphaFoldDB; Q6GFE2; -.
DR   SMR; Q6GFE2; -.
DR   KEGG; sar:SAR2007; -.
DR   HOGENOM; CLU_040293_0_0_9; -.
DR   OMA; IWNHQLI; -.
DR   OrthoDB; 1223596at2; -.
DR   PHI-base; PHI:3285; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; IEA:InterPro.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.1230.10; -; 1.
DR   Gene3D; 3.90.340.10; -; 1.
DR   Gene3D; 3.90.440.10; -; 1.
DR   InterPro; IPR017142; Nitric_oxide_synthase_Oase-su.
DR   InterPro; IPR044943; NOS_dom_1.
DR   InterPro; IPR044940; NOS_dom_2.
DR   InterPro; IPR044944; NOS_dom_3.
DR   InterPro; IPR004030; NOS_N.
DR   InterPro; IPR036119; NOS_N_sf.
DR   Pfam; PF02898; NO_synthase; 1.
DR   PIRSF; PIRSF037219; NOS_oxygenase; 1.
DR   SUPFAM; SSF56512; SSF56512; 1.
DR   PROSITE; PS60001; NOS; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..358
FT                   /note="Nitric oxide synthase oxygenase"
FT                   /id="PRO_0000170958"
FT   BINDING         62
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  41709 MW;  314C01C0432FDAFE CRC64;
     MLFKEAQAFI ENMYKECHYE TQIINKRLHD IELEIKETGT YTHTEEELIY GAKMAWRNSN
     RCIGRLFWDS LNVIDARDVT DEASFLSSIN YHIAQATNEG KLKPYITIYA PKDGPKIFNN
     QLIRYAGYDN CGDPAEKEVT RLANHLGWKG KGTNFDVLPL IYQLPNESVK YYEYPTSLIK
     EVPIEHDHYP KLRKLNLKWY AVPIISNMDL KIGGIVYPTA PFNGWYMVTE IGVRNFIDDY
     RYNLLEKVAD AFEFDTLKNN SFNKDRALVE LNYAVYHSFK KEGVSIVDHL TAAKQFELFE
     RNEAQQGRQV TGKWSWLAPP LSPTLTSNYH HGYDNTVKDP NFFYKKKKSN ANQCPFHH