ID   NOSO_DEIRA              Reviewed;         356 AA.
AC   Q9RR97;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Nitric oxide synthase oxygenase;
DE            EC=1.14.14.47 {ECO:0000250|UniProtKB:O34453};
DE   AltName: Full=NOSoxy-like protein;
GN   Name=nos; OrderedLocusNames=DR_2597;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   FUNCTION, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=11756668; DOI=10.1073/pnas.012470099;
RA   Adak S., Bilwes A.M., Panda K., Hosfield D., Aulak K.S., McDonald J.F.,
RA   Tainer J.A., Getzoff E.D., Crane B.R., Stuehr D.J.;
RT   "Cloning, expression, and characterization of a nitric oxide synthase
RT   protein from Deinococcus radiodurans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:107-112(2002).
RN   [3]
RP   INTERACTION WITH TRPS2, AND ACTIVITY OF THE COMPLEX.
RX   PubMed=15520379; DOI=10.1073/pnas.0405483101;
RA   Buddha M.R., Keery K.M., Crane B.R.;
RT   "An unusual tryptophanyl tRNA synthetase interacts with nitric oxide
RT   synthase in Deinococcus radiodurans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15881-15886(2004).
RN   [4]
RP   NITRATION OF TRYPTOPHAN.
RX   PubMed=15466862; DOI=10.1074/jbc.c400418200;
RA   Buddha M.R., Tao T., Parry R.J., Crane B.R.;
RT   "Regioselective nitration of tryptophan by a complex between bacterial
RT   nitric-oxide synthase and tryptophanyl-tRNA synthetase.";
RL   J. Biol. Chem. 279:49567-49570(2004).
CC   -!- FUNCTION: Catalyzes the production of nitric oxide. The complex between
CC       TrpRS II and nitric oxide synthase oxygenase catalyzes the
CC       regioselective nitration of tryptophan at the 4-position.
CC       {ECO:0000269|PubMed:11756668}.
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:0000269|PubMed:11756668};
CC   -!- COFACTOR:
CC       Name=(6S)-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:57453;
CC         Evidence={ECO:0000269|PubMed:11756668};
CC   -!- ACTIVITY REGULATION: Nitric oxide synthase activity is increased by
CC       trpS2.
CC   -!- SUBUNIT: Homodimer. Forms a complex with trpS2; one homodimer of trpS2
CC       binds one homodimer of nos. {ECO:0000269|PubMed:11756668}.
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   -!- MISCELLANEOUS: Affinity for substrate L-arginine is increased by TrpRS
CC       II.
CC   -!- SIMILARITY: Belongs to the NOS family. Bacterial NOS oxygenase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE000513; AAF12132.1; -; Genomic_DNA.
DR   PIR; B75256; B75256.
DR   RefSeq; NP_296316.1; NC_001263.1.
DR   RefSeq; WP_010889221.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RR97; -.
DR   SMR; Q9RR97; -.
DR   STRING; 243230.DR_2597; -.
DR   EnsemblBacteria; AAF12132; AAF12132; DR_2597.
DR   KEGG; dra:DR_2597; -.
DR   PATRIC; fig|243230.17.peg.2842; -.
DR   eggNOG; COG4362; Bacteria.
DR   HOGENOM; CLU_040293_0_0_0; -.
DR   InParanoid; Q9RR97; -.
DR   OMA; IWNHQLI; -.
DR   OrthoDB; 1223596at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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; IDA:UniProtKB.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..356
FT                   /note="Nitric oxide synthase oxygenase"
FT                   /id="PRO_0000170954"
FT   BINDING         63
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   356 AA;  40022 MW;  3BF08E6DE3BEFECD CRC64;
     MSCPAAAVLT PDMRAFLRRF HEEMGEPGLP ARLRAVEEAG LWWPTSAELT WGAKVAWRNS
     TRCVGRLYWE ALSVRDLREL NTAQAVYEAL LQHLDDAFCG GHIRPVISVF GPGVRLHNPQ
     LIRYADDPIN ADFVDKLRRF GWQPRGERFE VLPLLIEVNG RAELFSLPPQ AVQEVAITHP
     VCLGIGELGL RWHALPVISD MHLDIGGLHL PCAFSGWYVQ TEIAARDLAD VGRYDQLPAV
     ARALGLDTSR ERTLWRDRAL VELNVAVLHS FDAAGVKLAD HHTVTAHHVR FEEREARAGR
     EVRGKWSWLV PPLSPATTPL WSRRYRAREE SPRFVRARCP FHTPTVHAST GHAPTG