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Database: UniProt
Entry: A0A1W6A026_9BACI
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ID   A0A1W6A026_9BACI        Unreviewed;       363 AA.
AC   A0A1W6A026;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=HM131_19595 {ECO:0000313|EMBL:ARI78893.1};
OS   Halobacillus mangrovi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=402384 {ECO:0000313|EMBL:ARI78893.1, ECO:0000313|Proteomes:UP000192527};
RN   [1] {ECO:0000313|EMBL:ARI78893.1, ECO:0000313|Proteomes:UP000192527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTB 131 {ECO:0000313|EMBL:ARI78893.1,
RC   ECO:0000313|Proteomes:UP000192527};
RA   Lee S.-J., Park M.-K., Kim J.-Y., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F.,
RA   Lee D.-W.;
RT   "The whole genome sequencing and assembly of Halobacillus mangrovi
RT   strain.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the production of nitric oxide.
CC       {ECO:0000256|ARBA:ARBA00002642, 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; CP020772; ARI78893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6A026; -.
DR   STRING; 402384.HM131_19595; -.
DR   KEGG; hmn:HM131_19595; -.
DR   OrthoDB; 3398374at2; -.
DR   Proteomes; UP000192527; 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   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}.
FT   DOMAIN          62..69
FT                   /note="Nitric oxide synthase (NOS)"
FT                   /evidence="ECO:0000259|PROSITE:PS60001"
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:0000256|PIRSR:PIRSR037219-1"
SQ   SEQUENCE   363 AA;  42453 MW;  5DFEFCF6C91439DE CRC64;
     MSKELYQEAE QFIRQCYEEL GKTDVEHRLA EIHQSIQDRG TYDHTFEELE YGAKIAWRNS
     NRCIGRLFWN SLKVFDHREL ESEQEIRDAL VDHIDYATNN GRIRSTISIF RPKLSGKEIR
     LWNHQLLRYA GYETDQGVIG DPASLAFTKK CQDLGWKGTE GSFDILPLVI QIDGKEPQWF
     DIPEEKILEV PLRHPEYDWF EDLGLKWYAV PIISDMELEI GGIHYTAAPF NGWYMETEIG
     ARNLADEFRY NLLPVVAEAM GLNTKRNSTL WKDRALIELN QAVIYSYKTD KVNIVDHHSA
     AQQFQLFENK ERKCGREATG DWTWLIPPIS PASTHIFHST YEDRVDTPNY FYQEKAYEKN
     PSD
//
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