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Database: UniProt
Entry: A7SA75_NEMVE
LinkDB: A7SA75_NEMVE
Original site: A7SA75_NEMVE 
ID   A7SA75_NEMVE            Unreviewed;      1118 AA.
AC   A7SA75;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333};
DE            EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333};
GN   ORFNames=NEMVEDRAFT_v1g110599 {ECO:0000313|EMBL:EDO39440.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO39440.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO39440.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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}.
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DR   EMBL; DS469607; EDO39440.1; -; Genomic_DNA.
DR   RefSeq; XP_001631503.1; XM_001631453.1.
DR   AlphaFoldDB; A7SA75; -.
DR   STRING; 45351.A7SA75; -.
DR   EnsemblMetazoa; EDO39440; EDO39440; NEMVEDRAFT_v1g110599.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_001570_16_0_1; -.
DR   InParanoid; A7SA75; -.
DR   OMA; KCPEPLR; -.
DR   PhylomeDB; A7SA75; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
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; 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   3: Inferred from homology;
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:UP000001593}.
FT   DOMAIN          483..621
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          677..927
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         144
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   1118 AA;  125752 MW;  60111B51A1147016 CRC64;
     MNGVASGILR CPFSQFSEHA KSPKYVKLKN WVTGQQYTDT LHQKSKTRMH CTAARCEGSL
     MRPYGGENPS PRPYGIPRPK EEVREHAVDF LEQYYTSMKM NNSPAHEKRL AEVLKDIEAT
     GSYDLTEKEL MFGARMAWRN ASRCIGRIQW NRLHLFDARD VFTARGMYEA IIRHIKYGTN
     KGNIRSTITV FPHRREPHKD FRVWNTQLIQ YAGYKQPDGS VIGDPAGLEL TEICVALGWK
     PKGGRFDVLP LVLQAGGERP EYFEIPEDLI LEVKLKHPKY DWFEELGLRW YALPAVSCLC
     LDVGGIEFPG CPFNGWYMVT EIGARDLGDP CRYNMLEPVA KKLGLDTKSN ASLWKDISCV
     EINVAVLYSF QATGVTITDH HTASETFMKH FENETKLRGG CPGDWVWVVP PLSGSVSPVF
     HQEMLNYMLK PSYEYQDDPW KHYKITTAES NSDRKKLSFK EVAKAVKFSA NLMGKAMAKR
     TKAIILYATE TGKSESYARM LADLFLHAFD PKVMRMDEYP HPEMENEQLI LIVTSTFGNG
     DPPENGEVST INPLDSASQQ RIIEDQMFGL GSRAYPNFCA FARSLDKIIQ ELGAEQIHKC
     GEGDELAGQE ESFKTWAKQV FKAACDTFCV GEMVNVAEAD ESLNTLSSGW SPGKYRFTSV
     KEELQDVCKS IASVNNKPIV GAKVKSVKKL QSADSSRSTI LLKLDTSPAA EFHYNPGDHL
     SVFPCNRREL VQSLIDRLCE APDPDQPIKL EVCQETSGKR PFGKTKKWTP VDRLPTPTTV
     REAFSRFIDI AGTPTPQILK SLASLATNPK DREALETLGK GDNHYDDWKY EKQSNIVEVL
     EEFPSVNVEA EMLLTQLPLL QPRFYSISSS QDFSPNEVHL TVAVVQYNKR EGKGPVHYGV
     CSTWFNGLKP GDIVPCFVRK AHSFHLPDDG SLPIIMVGPG TGIAPFRSFW QQRQYDIVKK
     PSPVPKPRDA APGSGWGDMV LYFGCRCSTL DDIYQEETKT AHQDGALAAV RTALSREPGH
     VKQYVQDLLK EDADAIIDKL VGQGAHLYTC GDVSMAADVC RTIQKLLEEY AAMTQQEAQE
     FIDNLKSSGR YHEDIFGVTL RTREVTNRVR TAARKYVV
//
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