ID M3ZK07_XIPMA Unreviewed; 1420 AA.
AC M3ZK07;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333};
DE EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000002549.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000002549.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000002549.1};
RG Ensembl;
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 -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267,
CC ECO:0000256|PIRNR:PIRNR000333}.
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DR RefSeq; XP_005803890.1; XM_005803833.1.
DR Ensembl; ENSXMAT00000002554.2; ENSXMAP00000002549.1; ENSXMAG00000002504.2.
DR GeneID; 102233853; -.
DR KEGG; xma:102233853; -.
DR CTD; 4842; -.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000159357; -.
DR HOGENOM; CLU_001570_16_0_1; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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 CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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 Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF000333; NOS; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00228; PDZ; 1.
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; SSF50156; PDZ domain-like; 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.
DR PROSITE; PS50106; PDZ; 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:UP000002852};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 17..99
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 746..926
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 981..1228
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 406
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 1420 AA; 160002 MW; C609A1E62E720C54 CRC64;
MQESEPTVCQ LQPNIISVRL FKRKVGGLGF LVKQRVSKPP VIVSDLIRGG AAEECGLVQV
GDIVLAVNNK PLVDLSYERA LETLKNVSPE SHAVLILRGP EGFTTHLETT LTRDGRQRTV
RITRPAFPPS KSFDQWSPLS AYSPGQQLSK EPQLRAIENL SSPSITQTLL QRGGMQGQDG
GRGALLCNGL EENNDLLKEI EPVLHLIKNS KKEINGEGQR NAGRRDAEIQ VAWDLSVGNE
TSIQLGSDND RMLKDVPVAD HNADIDKSTA QGRISPIKSV QNGSPSKCPR YIKIKNWETG
TVYNDVLHHG CSKMPICSEN VCNGSVMVPS QGVHKPDEVR TKEELLPLAA DFIDQYYTSI
KRYGSKAHVD RWEEVTKEIE ASGTYQLKDT ELIYGAKHAW RNAARCVGRI QWSKLQVFDA
RDCTTAHGMY NYICNHIKYA TNKGNLRSAI TIFPQRTDGK HDFRVWNSQL IRYAGYKQPD
GGILGDPANV EFTEICMQLG WKAPKGRFDV LPLLLQANGN DPELFEIPED LILEVPIIHP
KFEWFKDLEL KWYGLPAVAN MLLEIGGLEF TGCPFSGWYM GTEIGVRDFC DSSRYNILEE
VANKMGLDTR KTSSLWKDQA LVEINIAVLH SFQTCKVTIV DHHSATESFM KHMENEYRVR
GGCPGDWVWI VPPMSGSITP VFHQEMLNYR LTPSFEYQPD PWNTHVWKGV NGTPTKKRAI
GFKKLAKAVK FSAKLMGQAM AKRVKATILF ATETGKSQDY AKTLCEIFKH AFDAKVISMD
EYDVVDLEHE TLVLAVTSTF GNGDPPENGE KFGAALMEMR HPTSNTEDRK SYKVRFNSVS
SYSDTRKSSS DEPEARINFE STGPLANVRF SVFGLGSRAY PHFCAFAHAV DTLFEELGGE
RILRMGEGDE LCGQEESFRT WAKKVFKAAC DVFCVGDDVN IEKANDSLIS NDRSWKKSKF
RLTYTAEAPA LTEALYSVQK KKVYGAMMIE AQNLQSSKSN RSTILVRLDT NNHDSLRYKP
GDHLGIFPGN HEDLVTALID KLEDAPPVNQ IVKVEFLEER NTALGVISNW TSETRIPPCT
INQAFQYFLD ITTPPTPVLL QQFAALATND KQKRKLEILS KGLQEYEEWK WYNNPTLVEV
LDEFPSIQMP STLLLTQLPL LQPRYYSISS SPDLYSGEIH LTVAVVSYRT RGGQGPIHHG
VCSSWLNRIE KGEMVPCFVR SAPSFQLPKD NKAPCILVGP GTGIAPFRSF WQQRQYDLEQ
NGIKSCPMIL VFGCRQSEMD HIYKEETLQA KNREVFKELY AAYSREPGKP KKYVQDVLRE
HLSETVYQCL RKEGGHIYVC GDVTMAGDVL KTIQQIIKQQ GQMSIEDAGF YISKLRDENR
YHEDIFGVTL RTYEVTNRLR SESIAYIEEN KKDSDEVFCS
//
