ID A0A109QE05_9BACL Unreviewed; 352 AA.
AC A0A109QE05;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ASO14_2744 {ECO:0000313|EMBL:AMA64576.1};
OS Kurthia sp. 11kri321.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA64576.1, ECO:0000313|Proteomes:UP000058129};
RN [1] {ECO:0000313|EMBL:AMA64576.1, ECO:0000313|Proteomes:UP000058129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11kri321 {ECO:0000313|EMBL:AMA64576.1,
RC ECO:0000313|Proteomes:UP000058129};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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; CP013217; AMA64576.1; -; Genomic_DNA.
DR RefSeq; WP_068456508.1; NZ_CP013217.1.
DR AlphaFoldDB; A0A109QE05; -.
DR STRING; 1750719.ASO14_2744; -.
DR KEGG; kur:ASO14_2744; -.
DR PATRIC; fig|1750719.3.peg.2704; -.
DR OrthoDB; 3398374at2; -.
DR Proteomes; UP000058129; 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; 3.90.440.10; 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.
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:UP000058129}.
FT DOMAIN 2..348
FT /note="Nitric oxide synthase (NOS)"
FT /evidence="ECO:0000259|Pfam:PF02898"
FT BINDING 58
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 352 AA; 40755 MW; E40B9EA7B65048CB CRC64;
MLEKARAFIK QFGKEMKKPI EQRLKEIEEE IISTGTYTHT EEELVYGAKV AWRNSNKCIG
RLFWNSLHVF DHRRLEDEEE IFEALVEHIR YATNGGKIRP TISIFAPGRV RIWNDQLIRY
AGYEKDGQVI GDTVSLDVTK KFHELGFPMG DQPYDILPLV IQVDDRPPKM FSIPKDAILE
VPITHSQYPK VEQIGMRWYA VPIISNMGYE VGGITYEAAP FNGWYMGTEI GARNLADEDR
YNFLPQVAEA IGIEAKRAHT LWKDRALVEL NYAVLESYKQ AGVSIVDHHT AAQQFQLFEQ
QEEKEGRDVT GNWTWLIPPL SPATTHIFHR PYNNTKKSPN YIYQQKPFHL EK
//
