ID A0A098TK07_9CYAN Unreviewed; 376 AA.
AC A0A098TK07;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, 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=DO97_07005 {ECO:0000313|EMBL:KGF72665.1};
OS Neosynechococcus sphagnicola sy1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC Neosynechococcaceae; Neosynechococcus.
OX NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF72665.1, ECO:0000313|Proteomes:UP000030170};
RN [1] {ECO:0000313|EMBL:KGF72665.1, ECO:0000313|Proteomes:UP000030170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF72665.1,
RC ECO:0000313|Proteomes:UP000030170};
RA Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., Sanges R.;
RT "Evolution of Synechococcus.";
RL Mol. Ecol. 0:0-0(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF72665.1}.
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DR EMBL; JJML01000021; KGF72665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098TK07; -.
DR STRING; 1497020.DO97_07005; -.
DR Proteomes; UP000030170; 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.
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:UP000030170}.
FT DOMAIN 7..359
FT /note="Nitric oxide synthase (NOS)"
FT /evidence="ECO:0000259|Pfam:PF02898"
FT BINDING 66
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 376 AA; 43706 MW; 98A36415E595A1C1 CRC64;
MQPIGSIKAE AEVFLKQCYI DEGIAPIFPY RWEDVEEEIA ETGTYQQTYD ELVYGAKLAW
RNSNRCLGRN FWHNLHVRDM RHLETEVEMF QAILEHIQFA TNGGEIRATI TIFKPDGRRF
WNPQYFQYAG YRQPDRSILG DPGNVELTDQ AMRLGWHPES QTRFDYLPLI IQLPGQEPRW
FEIPPQLILE VPLTHPRYDW FGDLRLKWYG LPAVSNMVFD VGGIQYTAAP FNGFYMGAEI
GARNFGDHHR YNMLPVIAER MGLDCSQNST LWRDLALVEL NIAVLFSYHQ QEVRLLDHHT
LTESFMQFAD SEHQAGRLVQ ADWGCLVPPL SASTTPVFHT QFDGNRILKP NFFYAPLPWQ
RVAQSPGCPF HHEWPD
//
