NOSO_STAAS
ID NOSO_STAAS Reviewed; 358 AA.
AC Q6G818;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=SAS1838;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571857; CAG43643.1; -; Genomic_DNA.
DR RefSeq; WP_000897635.1; NC_002953.3.
DR AlphaFoldDB; Q6G818; -.
DR SMR; Q6G818; -.
DR KEGG; sas:SAS1838; -.
DR HOGENOM; CLU_040293_0_0_9; -.
DR OMA; IWNHQLI; -.
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_0000170959"
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; 41710 MW; 349A3A83E8D643A1 CRC64;
MLFKEAQAFI ENMYKECHYE TQIINKRLHD IELEIKETGT YTHTEEELIY GAKMAWRNSN
RCIGRLFWDS LNVIDARDVT DEASFLSSIT YHITQATNEG KLKPYITIYA PKDGPKIFNN
QLIRYAGYDN CGDPAEKEVT RLANHLGWKG KGTNFDVLPL IYQLPNESVK FYEYPTSLIK
EVPIEHNHYP KLRKLNLKWY AVPIISNMDL KIGGIVYPTA PFNGWYMVTE IGVRNFIDDY
RYNLLEKVAD AFEFDTLKNN SFNKDRALVE LNYAVYHSFK KEGVSIVDHL TAAKQFELFE
RNEAQQGRQV TGKWSWLAPP LSPTLTSNYH HGYDNTVKDP NFFYKKKESN ANQCPFHH