ID   NOS_BOMMO               Reviewed;        1209 AA.
AC   Q8T8C0; Q9BLL0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Nitric oxide synthase {ECO:0000312|EMBL:BAB85836.1};
DE            EC=1.14.13.39;
DE   AltName: Full=Inducible nitric oxide synthase-like protein;
GN   Name=NOS {ECO:0000312|EMBL:BAB85836.1};
GN   Synonyms=iNOS-LP {ECO:0000312|EMBL:BAB33296.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAB85836.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=Tokai X Asahi {ECO:0000269|PubMed:12000645};
RC   TISSUE=Larva {ECO:0000269|PubMed:12000645};
RX   PubMed=12000645; DOI=10.1046/j.1365-2583.2002.00333.x;
RA   Imamura M., Yang J., Yamakawa M.;
RT   "cDNA cloning, characterization and gene expression of nitric oxide
RT   synthase from the silkworm, Bombyx mori.";
RL   Insect Mol. Biol. 11:257-265(2002).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAH23563.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Reproductive system {ECO:0000312|EMBL:BAH23563.1};
RA   Nagaoka S., Takata Y.;
RT   "Identification of nitric-oxide synthase from Bombyx mori.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAH23563.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-354.
RA   Yang J., Taniai K., Yamakawa M.;
RT   "Inducible nitric oxide synthase-like protein(iNOS-LP) cDNA.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC       diverse functions throughout the body. Involved in the induction of
CC       immune gene expression. {ECO:0000269|PubMed:12000645, ECO:0000305}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P29475};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29475};
CC       Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29475};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P29475};
CC       Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P29475};
CC   -!- ACTIVITY REGULATION: Expression is dependent on and stimulated by
CC       NADPH, calcium, BH4 and calmodulin. The activity is not dependent on
CC       FAD and is not stimulated by its presence.
CC       {ECO:0000269|PubMed:12000645}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed at a low level in the
CC       larval fat body, hemocyte, Malpighian tubule, midgut, silk gland and
CC       adult antenna. {ECO:0000269|PubMed:12000645}.
CC   -!- INDUCTION: Induced strongly in the fat body by lipopolysaccharide
CC       (LPS). {ECO:0000269|PubMed:12000645}.
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000255}.
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DR   EMBL; AB071182; BAB85836.1; -; mRNA.
DR   EMBL; AB485775; BAH23563.1; -; mRNA.
DR   EMBL; AB017521; BAB33296.1; -; mRNA.
DR   RefSeq; NP_001036963.1; NM_001043498.1.
DR   AlphaFoldDB; Q8T8C0; -.
DR   SMR; Q8T8C0; -.
DR   STRING; 7091.Q8T8C0; -.
DR   PaxDb; 7091-BGIBMGA002938-TA; -.
DR   EnsemblMetazoa; GeneID_692510M_001043498.1; NP_001036963.1; GeneID_692510OS1.
DR   GeneID; 692510; -.
DR   KEGG; bmor:692510; -.
DR   CTD; 4842; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; Q8T8C0; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000005204; 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   CDD; cd00795; NOS_oxygenase_euk; 1.
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; 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; 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   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.
DR   PROSITE; PS60001; NOS; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1209
FT                   /note="Nitric oxide synthase"
FT                   /id="PRO_0000403313"
FT   DOMAIN          521..723
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          776..1021
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          491..511
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P29475, ECO:0000255"
FT   REGION          603..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         181
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         244
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         353
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         354
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         358
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         363
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         444
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         457
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         472
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         527..531
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         669..700
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   BINDING         811..822
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         954..964
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         1028..1147
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         1128..1143
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   CONFLICT        157
FT                   /note="R -> K (in Ref. 3; BAB33296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="F -> L (in Ref. 3; BAB33296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="T -> I (in Ref. 3; BAB33296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="A -> P (in Ref. 3; BAB33296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340..341
FT                   /note="CG -> KK (in Ref. 3; BAB33296)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351..352
FT                   /note="NG -> KN (in Ref. 3; BAB33296)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1209 AA;  137507 MW;  92A73F04B12C2E2C CRC64;
     MSNFFKICCV KDPGGSAKEN LRKMDQVNGH FVSATCPFSG ESVELKVDSN QKQVKPNLRI
     KVPQPIRLKN HVAHDENFDT LHSRINEVTH FNTKCSEKVC QTSIMDIPGR GDTPRTAEEV
     FKDAQAFLTQ YYASIKRENS EAHKARLDEV KRELKERGTY QLKTSELVFG AKLAWRNATR
     CIGRIQWKKL QIFDCREVTT ASGMFEALCN HIKYATNKGN IRSAITIFPQ RTDGKHDYRI
     WNPQLINYAG YQEPDGSITG DPARVEFTEI CMKLGWKAPR TPWDILPLVL SADGKDPEFF
     ELPKEIVMEV QFEHPEYDWF KDMGWKWYAL PAVSNMRLAC GGLEFTANSF NGWYMGTEIG
     CRNLCDESRL NIVEAVAKKM GLDTNSFVSL WKDKALVEVN IAVLHSFHRD NVSIVDHHSA
     SEQFQKHLEN ENKSRGGCPA DWIWIVPPMS SSLTTVFHQE MALYYIRPSY DYQEPPWKTH
     QWTKSDGTKT VHRKFHFKQI ARAVKFTSKL FGRALSKRIK ATILYATETG KSEHYAKELG
     TIFGHAFNAQ VHCMSEYDMF SIEHETLVLI VASTFGNGEP PANGVDFAEH LFQMLYNETN
     NNRGDGTSDL GSGTFKTPTP KSLMRSNSMM TPSFEYKRQL TRLESNKSSV AGASSIEQIG
     PLSNVCFAVF GLGSSAYPKF CHFGKTVDKI LGDLGGERIL ELACGDELYG QEQQFRAWSS
     KIFQVACETF CLDENGMVKD AKKALGDVPL TEETVRFGKY QGDTKLKAAL EASFRKQLIT
     CKVKENKNLG DFSADRATVF VDMQPETEFK YDPGDHVGVL ACNRKEIVDA VLERMKDVDD
     YDKTVQLQVM KETLTPTGAI KTWEQHERLP AVTIRQIFTR FLDITTPPST TVLKYLSKAC
     TDQNDAAQLK ELAIDSNKYD DWRHLHYPHL AEVLAQFPSC RPQASLLAAL LPSLQPRFYS
     ISSSPLAHPH RIHITCAVVV YRTQNGQGPM HYGVCSTYLQ NLKPEDEALV FIRRAPSFHM
     PKDLSAPLIL VGPGSGIAPF RGFWHHRKHQ IKNLIPNKQK PGPVWLFFGC RNRGMDLYKE
     EKEKALADGV LSKVFLALSR EDSVEKKHIQ TLLEDEGAEI SRMLLDENGH FYVCGDCKMA
     EEVQQKLKEI MKKHAKMTEQ EYEEFILNLM DENRYHEDIF GITLRTAEVQ SASREFAKRT
     RQESQKSQT
//