NOSO_STAAC
ID NOSO_STAAC Reviewed; 358 AA.
AC Q5HEK7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SACOL1976;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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}.
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DR EMBL; CP000046; AAW36946.1; -; Genomic_DNA.
DR RefSeq; WP_000897635.1; NC_002951.2.
DR AlphaFoldDB; Q5HEK7; -.
DR SMR; Q5HEK7; -.
DR EnsemblBacteria; AAW36946; AAW36946; SACOL1976.
DR KEGG; sac:SACOL1976; -.
DR HOGENOM; CLU_040293_0_0_9; -.
DR OMA; IWNHQLI; -.
DR Proteomes; UP000000530; 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_0000170955"
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