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Database: UniProt
Entry: A0A091K868_COLST
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ID   A0A091K868_COLST        Unreviewed;       815 AA.
AC   A0A091K868;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE            EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
DE   Flags: Fragment;
GN   ORFNames=N325_07765 {ECO:0000313|EMBL:KFP33205.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP33205.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP33205.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP33205.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC         + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00035595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000256|ARBA:ARBA00035595};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950};
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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DR   EMBL; KK548985; KFP33205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091K868; -.
DR   Proteomes; UP000053615; Unassembled WGS sequence.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; -; 2.
DR   Gene3D; 6.10.250.410; -; 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; IPR001094; Flavdoxin-like.
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; IPR012144; NOS_euk.
DR   InterPro; IPR004030; NOS_N.
DR   InterPro; IPR036119; NOS_N_sf.
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; PF02898; NO_synthase; 1.
DR   PIRSF; PIRSF000333; NOS; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
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   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
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:UP000053615}.
FT   DOMAIN          300..479
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          534..781
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP33205.1"
FT   NON_TER         815
FT                   /evidence="ECO:0000313|EMBL:KFP33205.1"
SQ   SEQUENCE   815 AA;  92404 MW;  8F9897232165D86C CRC64;
     RSAITIFPQR TDSKHDFRIW NAQLIRYAGY KLPDGTILGD PANVELTEIC IQQGWKAPHG
     RFDILPLLLQ ANGNDPELFE IPPELVLEVP IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG
     GLEFSACPFS GWYMGTEIGV RDYCDNSRYN ILEQVAKKMN LDMRKTSSLW KDQALVEINI
     AVLYSFQSDK VTIVDHHSAT ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM
     LNYRLTPSFE YQPDPWNTHV WKGVNGTPTK KRAIGFKKLA KAVKFSAKLM GQAMAKRVKA
     TILYATETGK SQVYAKTLCE IFKHAFDAKV LYQLPWCKIM HVAGILSPEL WFGLFPSVEP
     SEHTAWGEPH SPLLTLDAVA VHRSYKVRFN SVSSYSDARK SSSDGPDSRD NFESTGPLAN
     VRFSVFGLGS RAYPHFCAFA RAVDTLLEEL GGERILRMGE GDELCGQEES FRTWAKKVFK
     AACDVFCVGD DVNIEKANNS LISNDRSWKR SKFRLTYVAE APELTQGLYS IHKKRVYAAR
     LITRQNLQSP KSSRLTIFLR LHTDGHQELQ YLPGDHLGVF PGNHEDLVNA LIDRLEDAPP
     ANQLVKVELL EERNTALGVI SNWTDENRVP PCTIFQAFKY YLDITTPPTP LLLQQFALLA
     TSDKEKKRLQ VLSKGLQEYE EWKWSKNPTI VEVLEEFPSV QMPSTLLLTQ LPLLQPRYYS
     ISSSPEMYPG EVHLTVAVVS YRTRDGEGPI HHGVCSSWLN RIQPDEVVPC FVRGAPGFHL
     PQDPQVPCIL IGPGTGIAPF RSFWQQRLFD IKHKG
//
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