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Database: UniProt
Entry: A0A1G8SNR9_9ACTN
LinkDB: A0A1G8SNR9_9ACTN
Original site: A0A1G8SNR9_9ACTN 
ID   A0A1G8SNR9_9ACTN        Unreviewed;       384 AA.
AC   A0A1G8SNR9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Nitric oxide synthase oxygenase {ECO:0000256|ARBA:ARBA00018859, ECO:0000256|PIRNR:PIRNR037219};
DE            EC=1.14.14.47 {ECO:0000256|ARBA:ARBA00012735, ECO:0000256|PIRNR:PIRNR037219};
GN   ORFNames=SAMN05421874_101395 {ECO:0000313|EMBL:SDJ30906.1};
OS   Nonomuraea maritima.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=683260 {ECO:0000313|EMBL:SDJ30906.1, ECO:0000313|Proteomes:UP000198683};
RN   [1] {ECO:0000313|EMBL:SDJ30906.1, ECO:0000313|Proteomes:UP000198683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDJ30906.1,
RC   ECO:0000313|Proteomes:UP000198683};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the production of nitric oxide.
CC       {ECO:0000256|PIRNR:PIRNR037219}.
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:0000256|ARBA:ARBA00000737};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR037219, ECO:0000256|PIRSR:PIRSR037219-1};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037219}.
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. {ECO:0000256|PIRNR:PIRNR037219}.
CC   -!- SIMILARITY: Belongs to the NOS family. Bacterial NOS oxygenase
CC       subfamily. {ECO:0000256|ARBA:ARBA00005411,
CC       ECO:0000256|PIRNR:PIRNR037219}.
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DR   EMBL; FNFB01000001; SDJ30906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8SNR9; -.
DR   STRING; 683260.SAMN05421874_101395; -.
DR   OrthoDB; 3398374at2; -.
DR   Proteomes; UP000198683; Unassembled WGS sequence.
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   CDD; cd00575; NOS_oxygenase; 1.
DR   Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 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   PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   Pfam; PF02898; NO_synthase; 1.
DR   PIRSF; PIRSF037219; NOS_oxygenase; 1.
DR   SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR   PROSITE; PS60001; NOS; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR037219};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR037219};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037219};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR037219};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198683}.
FT   DOMAIN          91..98
FT                   /note="Nitric oxide synthase (NOS)"
FT                   /evidence="ECO:0000259|PROSITE:PS60001"
FT   BINDING         92
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:0000256|PIRSR:PIRSR037219-1"
SQ   SEQUENCE   384 AA;  43496 MW;  0046EB4149DD5586 CRC64;
     MTESADCRVP TWIRSLRPFD VPAARPVAAR SIDLREAERF IRLYHAENPS VGGLHARLRD
     IARDVARYGT YTHSFEELEF GARVAWRNSN RCIGRLYWRS LKVRDRRLVS APEGVALESV
     AHLHEATNKG KIRPTITIMA PDTPALRAPR IRNDQLIRYA GYRTEDGVVG DPRNVDLTEY
     AQKLGWEGKG GRFDVLPLII EPPFGEPLLC HLPGDAVLEV PIVHPEYAWF EELGLRWHAV
     PAISDMCLEI GGICYPCAPF NGWYMGTEIG ARNFADTDRY DRLGAVAERL GLDTSTERSL
     WRDHALVELN VAVLHSFERA GVTITDHHTE SRRFLAHLAK EEKAGRVCPA DWSWIVPPMS
     GGVTPVFHRY YDTRELTPAF VHHH
//
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