ID Q8MU49_DISST Unreviewed; 1115 AA. AC Q8MU49; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 24-JUL-2024, entry version 109. DE RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333}; DE EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333}; OS Discosoma striata (Striped mushroom). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Corallimorpharia; OC Discosomidae; Discosoma. OX NCBI_TaxID=105400 {ECO:0000313|EMBL:AAK61379.1}; RN [1] {ECO:0000313|EMBL:AAK61379.1} RP NUCLEOTIDE SEQUENCE. RA Panchin Y.V., Sadreyev R.I., Moroz L.L.; RT "Nitric oxide synthase (NOS) from Cnidaria: the search for the NOS RT prototype."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. 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|PIRNR:PIRNR000333}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY036119; AAK61379.1; -; mRNA. DR AlphaFoldDB; Q8MU49; -. DR SMR; Q8MU49; -. 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; cd06202; Nitric_oxide_synthase; 1. 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; IPR050607; NOS. 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}. FT DOMAIN 488..628 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT DOMAIN 684..932 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT BINDING 153 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 1115 AA; 125377 MW; 4D32D67835B02D24 CRC64; MKEIKVPECP FIGADEKKCP FAAGFQMRSQ EPKYLRVNNW IEGTQMVDTL HQKATNPLHC TNGRCTGSIM YPYGGEIPEA RPYGIPRPKD EVITHAQDFL EQLYSAKKLS DSQEHLQRRT EVMKAVKETG TYHLTEDELI FASKTAWRNA ARCIGRIQWN NLQLFDARHV KTAKEMFEAI KKHLVYATNE GNLRSAITVF PQRKESKKDF RVWNPQLIRY AGYKHLDGTV VGDPASVDFT ELCQSLGWKG KGGRFDILPL VLQANGGPPE CFELPDELAL QVKIKHPKYP WFEKLGLRWY ALPAVSNMML DAGGLEFTAA PFNGWYMVTE IGTRDLADQQ RYNMLEPIAK KMGPDTKSNA SLWKDFALVE LNYAVMYSFQ EAGVTLADHH STSESFMKHM EKEIKLRGGC PADWVWIVPP LSGGATPVFH QEMLNYSLKP SYEYQPDPSN FYSITGKPIT KTSFKAVAKA TLFSAFLMRK VLSKRKKATV LFATETGRSE GFARNLGKLL SHAFDVKVLC MADYEHVQLK DEKLLFVVAS TFGNGDPPEN GASFATFLHS MGNAQPLRNL RYSVFGLGSR AYPNFCNFGH YMDDHLKKLG GERILSMGEG DELCGQDESF KEWAKNVFKG ACDVFGMKKE ASNKVVTLSL ENMSTGWGPG LYRWVTDRRK PKDLCSNLSR AYNKTVCPVK VISVKELQSR NSRRSTILVR FDVEKNKELN FEPGDHVAIF PANRANTVQD LIDMMHEKPT PDQPIRIEVA RENSGKPGGG RTWESFKRLP VACTLREALT RYLDISSVPT PQMMLYLSKL ATSPLEKLQL EALGKGGSRY GDWVLKKECN ILETLQAFPS VQVTADLLLT QLPLLQPRFY SISSSPDVHR NEIHATVAVV EYKKRGGQGP VHHGVCSTWL QGLTPGDTAA CYIRHAQSFH LPSDATVPVI LVGNGTGIAP FRGFWQQRMF DMNNKCLPDP QPGSRQRCGR WGEMALFFGC RNSQHDDVFR HEIEKAIYSK TISTVAKAFS REQGKPKRYV QDLLKEDAGN VCDLIVDSNA HVYVCGGAAM ANDVSKTIQN MLADRLSLSA DDALEYMRGL KSSNRYHEDV FGVAQRNKEP GGREN //