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Database: UniProt
Entry: K8F2G6_9CHLO
LinkDB: K8F2G6_9CHLO
Original site: K8F2G6_9CHLO 
ID   K8F2G6_9CHLO            Unreviewed;      1080 AA.
AC   K8F2G6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE            EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN   ORFNames=Bathy09g04630 {ECO:0000313|EMBL:CCO66498.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO66498.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO66498.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO66498.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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DR   EMBL; FO082270; CCO66498.1; -; Genomic_DNA.
DR   RefSeq; XP_007510938.1; XM_007510876.1.
DR   AlphaFoldDB; K8F2G6; -.
DR   SMR; K8F2G6; -.
DR   STRING; 41875.K8F2G6; -.
DR   GeneID; 19013969; -.
DR   KEGG; bpg:Bathy09g04630; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000198341; Chromosome_9.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
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   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF02898; NO_synthase; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT   DOMAIN          466..610
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          659..913
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1080 AA;  120596 MW;  0CDBD69002BEA74C CRC64;
     MADEDECSNV LPVSRCPFGH GTATVDPYPG YVHGKHPAVC PRGCVPLKAD VSKAEAPKDK
     LKREATEFIE LYGKENKVSE EDTMRRVAEV LESIESTGTY THTIDEIRHG ARVSWRNAPK
     CINRKFYNTL DVIDAREATT NEQMFEAIKT HLKRGIGADH IPVLMTVFRP QTPGMDDGPR
     IWNSQLIRYA GHRGNGEEVI GDPAELNFTD TVKKYFSWVP KSGSPGMFDC LPLVLQIDPK
     QPPSIFELPE ECLLEVPIHH PNVPEISSLG LKWYGIPAVS NITLDLGGLH YTAAPFNGWY
     MVTEIATRNF GDESRYNLLP KIAEAMGIDS STEETLWRDH ALAAVNFAVL YSFKRARVSI
     VDHHTAAASF AQWHAEELKK RGYCPGNWKW IIPPTASSTS SIYLGLNKMT EYTLKPALVG
     GMSAKSLVTR AIANGFFTPS GPGGSMMRAT LAVAKWSKRV RRVHGGVVLF ASDGGRTQSR
     ATWMWSFLRQ RLPMIRPVNI ANPDVDFKTA IGECGFIMLL ASTTGSGQIP TGSQLFLDWV
     NSDEGKDILK DKYFSVCAFG SKAYPKFCAG GKQFAAALRD VGASEMFNVV CIDQLDCEDV
     GVQKYMRSVF DWLLSKEKMT PGVNQLLKDS LASGKAIQPP FAIKLLAHDV HGKRTEYERP
     GVTATLVERE LLGSAERLST VSVTFELQDV RKGVEYYKPG DHVAVWPRTS EAQGRFFAAH
     FGIEYKEFIE IVSLEDSFFS LKLAIDPAIP RRVSVADLFT KILDINAEPP AEMLASLANY
     VDESECKQML EKLAREEDFR REWLEQTGVC VRTIFEQFPT LSTIHNRDKT VGVRMLQDIL
     LQIPKLRARF YSVSSAPDVC GNARFALTVG RLVYRSADNA RINLGFCSDF IATLSIGTNV
     TVELRPAPMF RMPKSNARPI IMLCAGTGIA PFKGFVDQLT VRSEPGAETW LIYGCRTRSN
     ELYAQDMRRA EQSGHLTKYL VAYSREEGQL KTYVDAKMRQ HADDIRRLVL NEDAHVYVCG
     DVRIETSVQT ALTEIMGGPE AFRALERSNK YHLDIFGAFD VQKQNENKLA NARKSLSMRE
//
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