ID A0A1Q2KUN8_9BACL Unreviewed; 356 AA.
AC A0A1Q2KUN8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=B0X71_01000 {ECO:0000313|EMBL:AQQ51834.1};
OS Planococcus lenghuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=2213202 {ECO:0000313|EMBL:AQQ51834.1, ECO:0000313|Proteomes:UP000188184};
RN [1] {ECO:0000313|EMBL:AQQ51834.1, ECO:0000313|Proteomes:UP000188184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y42 {ECO:0000313|EMBL:AQQ51834.1,
RC ECO:0000313|Proteomes:UP000188184};
RA Yang R.;
RT "The complete genomic sequence of a novel cold adapted crude oil-degrading
RT bacterium Planococcus qaidamina Y42.";
RL Submitted (FEB-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; CP019640; AQQ51834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2KUN8; -.
DR KEGG; pmar:B0X71_01000; -.
DR OrthoDB; 3398374at2; -.
DR Proteomes; UP000188184; 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.
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:UP000188184}.
FT DOMAIN 64..71
FT /note="Nitric oxide synthase (NOS)"
FT /evidence="ECO:0000259|PROSITE:PS60001"
FT BINDING 65
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 356 AA; 40808 MW; DC6F9B80F0551F84 CRC64;
MDTNLWQHAQ TFIELYYHEN DLPADRMTVR LDTVKEEIQR TGTYRHTAEE LTYGARVAWR
NSNRCIGRLF WQTLQVSDER EAQSAEDVFA ALERHVVSAY NNGKIRPLIT VFRPSGIRIR
NHQLLRYAGY ETAGDAHSKS FTAYCQRLGW KGAGTDFDLL PWVVQIGDQP PAWQEVPEHA
RPEVTIEHPE YAEFNDLNLK WYAVPVISDM KLEIGGIAYE AAPFNGWYMG TEIGARNLAD
EDRYNLLPAV AQYMGLDTRR LSSLWKDRAL IELNAAVLYS FKKAGVTIVD HHTAAKQFQT
FEQNEAAAHR DVTGNWVWLI PPVSPAATSI FHKRYDNAIK TPNFFHQPSS GDHREK
//
