ID Q1KYT1_MESAU Unreviewed; 1150 AA.
AC Q1KYT1;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333};
DE EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333};
GN Name=Nos2 {ECO:0000313|EMBL:ABC96767.1,
GN ECO:0000313|RefSeq:NP_001268573.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|EMBL:ABC96767.1};
RN [1] {ECO:0000313|RefSeq:NP_001268573.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15968502; DOI=10.1007/s00284-005-4503-z;
RA Ramirez-Emiliano J., Gonzalez-Hernandez A., Arias-Negrete S.;
RT "Expression of inducible nitric oxide synthase mRNA and nitric oxide
RT production during the development of liver abscess in hamster inoculated
RT with Entamoeba histolytica.";
RL Curr. Microbiol. 50:299-308(2005).
RN [2] {ECO:0000313|EMBL:ABC96767.1, ECO:0000313|RefSeq:NP_001268573.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16622021;
RA Perez L.E., Chandrasekar B., Saldarriaga O.A., Zhao W., Arteaga L.T.,
RA Travi B.L., Melby P.C.;
RT "Reduced nitric oxide synthase 2 (NOS2) promoter activity in the Syrian
RT hamster renders the animal functionally deficient in NOS2 activity and
RT unable to control an intracellular pathogen.";
RL J. Immunol. 176:5519-5528(2006).
RN [3] {ECO:0000313|RefSeq:NP_001268573.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [4] {ECO:0000313|RefSeq:NP_001268573.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.
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|PIRNR:PIRNR000333};
CC Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR000333};
CC Note=Binds 1 FMN. {ECO:0000256|PIRNR:PIRNR000333};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970,
CC ECO:0000256|PIRNR:PIRNR000333};
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267,
CC ECO:0000256|PIRNR:PIRNR000333}.
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DR EMBL; DQ355357; ABC96767.1; -; mRNA.
DR RefSeq; NP_001268573.1; NM_001281644.1.
DR STRING; 10036.ENSMAUP00000017510; -.
DR GeneID; 101823656; -.
DR KEGG; maua:101823656; -.
DR CTD; 4843; -.
DR eggNOG; KOG1158; Eukaryota.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000189706; Unplaced.
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; -; 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; 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; 2.
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 {ECO:0000256|ARBA:ARBA00022860,
KW ECO:0000256|PIRNR:PIRNR000333};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000333};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000333};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000333};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000333};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000333};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000333};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000333};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT DOMAIN 539..677
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 730..970
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 16..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
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:0000256|PIRSR:PIRSR000333-1"
SQ SEQUENCE 1150 AA; 130347 MW; 5F347E258EE89226 CRC64;
MACPWKFLFR AKSYQGDLKE EKDINNNVGK TPSAVPSPTT QDDPKGHRPA KHQNGSLQTL
TGTAQNGPEP LDKLHVSPST HPHHVKIKNW GSGETLQDTL HHKATSEFTC GSKSCLGSIM
NPKSLTRGPR DKPTSLEELL PQAIEFINQY YGSFTEAKIE EHLARVEAVT KDIETTGTYQ
LTRDELIFAT KLAWRNAPRC IGRIQWANLQ VFDARSCSTA QDMFQHICRH LLYATNNGNI
RSAITVFPQR SDGKHDFRIW NSQLIRYAGY QMPDGTIRGD PASLEFTQLC IDLGWKPRYG
RFDVLPLILQ ADGQDPEVFE IPPNLVLEVT MEHPKYEWFQ ELGLRWYALP AVANMLLEVG
GLEFPACPFN GWYMGTEIGV RDFCDTQRYN ILEEVGRRVG LETHTLASLW KDRAVTEINV
AVLHSFQKQN VTIMDHHTAS ESFMKHMHNE YRARGGCPAD WIWLVPPMSG SITPVFHQEM
LNYILSPFYY YQVEPWKTHI WQDGKLRPRR REIRLRVLVK AVLFASTLMR KAMASRVRAT
VLFATETGKS EVLARDLAAL FSYAFTTKVV CMNQYKASTL EDEELLLVVT STFGNGDCPS
NGQTLKKALF MLRELTHTFR YAVFGLGSSM YPQFCAFAHD IDQKLSQLGA SQLALTGEGD
ELSGQEDAFR SWAVQTFRAA CEAFDVRSKH HIQIPKRYTS NAVWEPQQYR LTQSPEPLDL
NKALSSIHAK NVFTMRLKSQ QNLQSEKSSR TTLLVQLSFE GSRGPSYLPG EHLGIFPGNQ
VALVQGILER VVDCPSPHQT MCLEVLDESG SYWVKDKRLP PCSLSQALTY FLDITTPPTQ
LQLHKLARLA TDEAERQRLE ALCQSSEYND WKFRNNPTFL EVLEEFPSLR VPAAFLLSQL
PILKPRYYSI SSSQDHTPSE VHLTVAVVTY RTRDGEGPLH HGVCSTWISS LKPQDPVPCF
VRSVSGFQLP EDPSLPCILI GPGTGIAPFR SFWQQRLHDF QNRGLKGGRM TLVFGCRHPE
EDHLYREEMQ EMAHKGVLHQ VHTAYSRLPG KPKVYVQDIL QKQLASEVLS VLHGEQGHLY
VCGDVRMARG VATTLKTLVA TKLNLNEEQV EDYFFQLKSQ KRYHEDIFSA VFSYGAKKGS
ALEQSKSTRL
//
