ID   NOS_SQUAC               Reviewed;         212 AA.
AC   Q9I9M2;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Nitric oxide synthase;
DE            Short=NOS;
DE            EC=1.14.13.39;
DE   Flags: Fragment;
OS   Squalus acanthias (Spiny dogfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Squalomorphii; Squaliformes; Squalidae; Squalus.
OX   NCBI_TaxID=7797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gill;
RA   Farmerie W.G., Holland K.P., Catches J.S., Morrison-Shetlar A.I.,
RA   Claiborne J.B. III, Edwards S.L., Evans D.H.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC       diverse functions throughout the body. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR   EMBL; AF232227; AAF36405.2; -; mRNA.
DR   AlphaFoldDB; Q9I9M2; -.
DR   SMR; Q9I9M2; -.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding;
KW   NADP; Oxidoreductase.
FT   CHAIN           <1..>212
FT                   /note="Nitric oxide synthase"
FT                   /id="PRO_0000170948"
FT   DOMAIN          60..>212
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   REGION          30..50
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          155..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         186..>212
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   NON_TER         1
FT   NON_TER         212
SQ   SEQUENCE   212 AA;  23651 MW;  3A6B115A679E6CFF CRC64;
     LNYQLSPSFE YQSDPWFTHV WKGVNGTPTK KRAIGFKKLA KAVKFSTKLM GQAMAKRVKA
     TILYATETGK SQVYAKTLCE IFKHAFDAKV MSMDEYDIVH LEHEALVLVV TSTFGNGDPP
     ENGEKFGSAL MEIRHPSSNS AERKSYKVRF NSVSSYSDSR KSSSDEPEHK DNFESTGPLA
     NVRFSAFGLG SRAYPHFCAF ARAVDTLLEE LG