NOS_RHOPR
ID NOS_RHOPR Reviewed; 1174 AA.
AC Q26240;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nitric oxide synthase, salivary gland;
DE Short=NOS;
DE EC=1.14.13.39;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RX PubMed=9022713; DOI=10.1111/j.1432-1033.1996.0807r.x;
RA Yuda M., Hirai M., Miura K., Matsumura H., Ando K., Chinzei Y.;
RT "cDNA cloning, expression and characterization of nitric-oxide synthase
RT from the salivary glands of the blood-sucking insect Rhodnius prolixus.";
RL Eur. J. Biochem. 242:807-812(1996).
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions throughout the body. The production of NO in the
CC salivary gland is used as a vasodilator for blood sucking.
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 -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR EMBL; U59389; AAB03810.1; -; mRNA.
DR AlphaFoldDB; Q26240; -.
DR SMR; Q26240; -.
DR STRING; 13249.RPRC003886-PA; -.
DR VEuPathDB; VectorBase:RPRC003886; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_16_0_1; -.
DR Proteomes; UP000015103; 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; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.1230.10; -; 1.
DR Gene3D; 3.90.340.10; -; 1.
DR Gene3D; 3.90.440.10; -; 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 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; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
DR SUPFAM; SSF63380; SSF63380; 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..1174
FT /note="Nitric oxide synthase, salivary gland"
FT /id="PRO_0000170952"
FT DOMAIN 505..693
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 745..990
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 475..495
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 162
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 225
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 334
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 335
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 339
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 344
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 425
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 438
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 453
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 639..670
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 780..791
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 923..933
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 998..1016
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 1095..1110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1174 AA; 132393 MW; C32F664EE51409CF CRC64;
MVHAECVWWL GIRILFVPPV SLEMHSVNVN NMSIQQQQQH QPQQQLLKPI RLANVSTQAQ
SLDTLHYKCQ QEGPCMEQAC LASVIYAGVN LKPRVRPKEE LLAHAKDFLD QYFASIRRLQ
SPAHEARWAQ VEKEVAATGT YELTETELVY GAKLAWRNAP RCIGRIQWAK LQVFDCRQVT
TTSGMFEALC NHIKYSTNKG NIRSAITIFP HRTDGKHDFR IWNKQLISYA GHKSKDGTVI
GDPACVEFTE ICIKLGWKGK GTMFDVLPLV LSANGEDPDY FDLPPELVFE VPLSHPKYKW
FSELGLKWFA LPAVSGMMFD CGGLQFTAAP FNGWYMNSEI GSRNLGDTNR YNMLEKIAQK
MELDTRTPVT LWKDLAMVEA NVAVLHSFQL HNVTIVDHHS AAESFMKHLE NEQRLRGGCP
ADWVWIVPPI SGSATPVFFQ EMANYFLYPG YIYQEDAWKC HEWKEIDVKH GLKKEKRKFH
FKQIARAVKF TSKLFGSALS KRIKATILFA TETGKSEMYA RKLGDIFSHA FHSQVLSMED
YDMSKIEHEA LLLVVASTFG NGDPPENGQG FAQSLYTIKM DENGLPNGHT NNTLASSASF
IKANSQTDRQ ASLERCDSFR GSTGDADVFG PLSNVRFAVF ALGSSAYPNF CAFGSYVDNL
LGELGGERLV KLTTGDEMCG QAQACNKWAP EVFSVACDTF CLDSDETFLE ATQMLHSEAV
TASTVRFVES ATQDLCKALS HLHNKKVWKC PLLGKRNLHG KGSTRATLLL EIERNENISY
QPGDHVGVLA CNRKELVEGI ISHLESAIDP DKSVQLQILK ENTTPDGIVR NWIPHDRLPT
CSLRTMLTRF LDITTPPSPN LLQFFASCAT NSEDQEKLTE LATDSAAYED WRYWKYPNLL
EVLEEFPSVR VLPALLIAQL TPLQPRFYSI SSAPSLYANQ IHLTVAVVQY CTQDGKGPIH
YGVASNYLYD VTIGDSIYLF TRSAPNFHLP KSDTAPIIMV GPGTGIAPFR GFWQHRLAQR
SLNGPGKFGK MSLFFGCRLR NLDLYQEEKE SMLKEGILSK VFLALSREPS IPKTYVQDLL
RVECKSVYIQ IVQEGGHFYV CGDCTMAEHV FRTLRQIIQD QGNMTDHQVD NFMLAMRDEN
RYHEDIFGIT LRTAEVHNRS RESARIRMAS QSQP
