ID A0A0L1JCA6_ASPNO Unreviewed; 1025 AA.
AC A0A0L1JCA6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN ORFNames=ANOM_002664 {ECO:0000313|EMBL:KNG89362.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89362.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG89362.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89362.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG89362.1}.
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DR EMBL; JNOM01000033; KNG89362.1; -; Genomic_DNA.
DR RefSeq; XP_015410285.1; XM_015547921.1.
DR AlphaFoldDB; A0A0L1JCA6; -.
DR SMR; A0A0L1JCA6; -.
DR STRING; 1509407.A0A0L1JCA6; -.
DR GeneID; 26804468; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 InterPro; IPR017927; FAD-bd_FR_type.
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; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
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; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF02898; NO_synthase; 1.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT DOMAIN 505..652
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 680..882
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1025 AA; 115031 MW; 493EECAE64975964 CRC64;
MQSTQVCEFQ TIIQKNPVLA STGCTPQFCQ AGRLIHSDEP RVGENRPLEV VKQEALGFLW
QLWQEGVYTE EQYTARHVEV LKSLEESEVI EPMVVDGVKT VGKTATWTQT PKELLHGIRL
AWKNSRKCIM RSHYMELDLC DLRHITTSAG MVKAVIQEAI KAFNKGQIRP TVFAFPPRST
SGTGPMFLSK QLLNFAGYRR DDGSILGDPS NVELTEDIIE LGWAPPEPRS HWDLLPIVAM
ADNDAPAWAD VPAELRDLVD IHHPRFENFQ KLGLKWYQFP ALSRLGFDIG GVQYTATPFI
GWYMDAEIGV RNLADSFRYN ALPDVAKALG FDIENYKKNP EYAEIEAMED LPDYEQLIWM
SRAQAELNYA VRWSFLQKGV SCIGTLAASS DWTRFDDEHA SKHGYRLNSD PYWIAPPQGS
IVPVWHRGGA PNYQPKPLIA RHRFDPVKSW RRRRDAVKAP VTRLVKVGED WVGAEHVTPV
QHKLCIANGT NALRNSVLAI PKRMVHIYYS STGTSALKLA EKLQRRVKEL PGGFHVDFNI
LNMLDLRKIK PSDPLLMVVS TTGDGRFPAN GAEFEAAMKD RAEEFNGALA VKYSILGVGD
SAYPTFNAAS VKLHEFMKSV GGIPIANGLT KGNTAVEALP MKAFNRWWSF VKDSLTGGGE
NAAPNESTED ECFEHYRMLE TFKKGRLLSK APAETGEGRI VMITMDLGDM DYIEMSHLRL
LPYNTPDQVG RALTALGVSN DDQRVPFMDS TMPGLSYKEF LQHYVDLEGK FKDLAWLSEA
FPAGDRWDTD GTVLDDLERF PALKQVSNEL RMKICLDMPL LRPRSFSVAS SAKYLGKGLV
EIMVRLHKGG RFSDKFLSAI SPGDSIRYSP VSIIPGQDLI SSEKHLIAIC TGTGFAPIRS
LLQQKIQVLK EAESQGMEFL FQSPPISIFV GFKAHDEALF EETLSTAERY GLIDMIFRVP
SNKQKRRVQH YVEDNKESVL AKIKEGSIYV CGAKAMVNDM AAKLSDMIGA DVRQNLGRRY
VEEIF
//
