ID G7VY69_PAETH Unreviewed; 374 AA.
AC G7VY69;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 OrderedLocusNames=HPL003_05435 {ECO:0000313|EMBL:AET57852.1};
OS Paenibacillus terrae (strain HPL-003).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET57852.1, ECO:0000313|Proteomes:UP000005876};
RN [1] {ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA Shin S.H., Kim S., Kim J.Y.;
RT "Complete sequence of Paenibacillus terrae HPL-003.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPL-003;
RA Shin S.H., Kim S., Kim J.Y.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AET57852.1, ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|EMBL:AET57852.1,
RC ECO:0000313|Proteomes:UP000005876};
RX PubMed=22328761; DOI=10.1128/JB.06668-11;
RA Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT Bacterium Isolated from Soil Found in Forest Residue.";
RL J. Bacteriol. 194:1266-1266(2012).
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; CP003107; AET57852.1; -; Genomic_DNA.
DR RefSeq; WP_014278603.1; NC_016641.1.
DR AlphaFoldDB; G7VY69; -.
DR STRING; 985665.HPL003_05435; -.
DR KEGG; pta:HPL003_05435; -.
DR eggNOG; COG4362; Bacteria.
DR HOGENOM; CLU_040293_0_0_9; -.
DR OrthoDB; 3398374at2; -.
DR Proteomes; UP000005876; 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 66..73
FT /note="Nitric oxide synthase (NOS)"
FT /evidence="ECO:0000259|PROSITE:PS60001"
FT BINDING 67
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 374 AA; 42341 MW; F5D7A6FD8BC1FF2D CRC64;
MEMKQQLLRE AEQFIYTCYE ELGRSRDEAE TRLLHIRHDI ETAGTYDHTH DELEHGAQMA
WRNSNRCIGR LFWDKLLVRD ARGASSTAEV VHELLEHIRI GTNGGKIKPT LTVFRSSKPG
QPDIRIWNHQ LIRYAGYESA EGVIGDPISV EFTNACRRMG WQGAMTPFDV LPLIVEAGGQ
PPELFDIPKH LVQEVPIEHP ELPGLASLGL RWYAVPMIAD MTLEIGGIVY TAAPFNGWYM
GTEIGARNFA DPFRYNMLPQ VAELMGLNIS SETTLWRDRA LVELNSAVLY SFKKAGVSIV
DHHTAAAQFR LFEEREAQAG RALTGDWTWL IPPLSPATTH IFHSSYDNRL VKPNFGVQEK
PYMQKKTQGC PFHS
//
