ID A0A0D1XAN5_9PEZI Unreviewed; 1165 AA.
AC A0A0D1XAN5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN ORFNames=PV09_09048 {ECO:0000313|EMBL:KIV99280.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99280.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV99280.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99280.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847580; KIV99280.1; -; Genomic_DNA.
DR RefSeq; XP_016209150.1; XM_016363039.1.
DR AlphaFoldDB; A0A0D1XAN5; -.
DR STRING; 253628.A0A0D1XAN5; -.
DR GeneID; 27317021; -.
DR VEuPathDB; FungiDB:PV09_09048; -.
DR HOGENOM; CLU_001570_16_1_1; -.
DR InParanoid; A0A0D1XAN5; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000053259; 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 Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
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; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_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; PF00258; Flavodoxin_1; 1.
DR Pfam; PF02898; NO_synthase; 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; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022643};
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:UP000053259}.
FT DOMAIN 579..729
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 756..964
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 129913 MW; 7824784E7C66343B CRC64;
MAVDYLDALN PTASTPSQCP AGFQTSAMIQ LTNDESLNAF DSSGEETGGG SETSSLTSSK
TSVGFGLTEV DSRSETDRDL KLSDHYVAEA MDGDGGRPPC LAGIKIYAKA QQEFERIRQA
HRTLAPTGCT PQFCQSGRMT RTNETRVGRD RPLAEIQQEA TDFLRECRDH GVIESDEHLQ
KRIDEALAQI LDSSIVTTVT DVNGNQRIDL AGGTWHQTTE ELEYGLRAAW RNSRRCIMRS
EHQSLTLYDF RNVHSSHDMA RAILDSMVEA FNRGHILPSA FIFPARLPGK RGPMVWNHQI
LAFAGYRMPD GSVLGDPANE EITNAIIKFG WKPPVNKSRW DLLPLVVMAE NDKPCMMEIP
LELQRTVRIT HPRYQREFKE LDLRWVLAPA LSRLGFDIGG NQYTASPFIG WFMDAEIGIR
NLADTFRYNS LPAIVQALSL SDDPSTPLDE LPEYKRLVAL SRAQAELNFA VYYSYMNEQV
TMTDSLTSSM EYQNYDEEYK ERTGFSLPAD PYWIAPPQGS IISLWHRGGL PNYQPKPLIC
KHVQDPVKAW TRESPDFERS CDKTSSSISS SPSVSRPTIQ IFFCSAGVSA RKMATKLHAT
MRKRVCGITG SFDVRSEQPL NKLDLAATGE EDIIFIISST TGRGAIPPNA QRFIERYQSA
ERMTSPPRFS CFGNGDSTYG DTYNASAKVV QELMVKLGCR SLFDDYFSGD TAVRNPDWES
FNRWTDAIDH LVFGAPKPTK ASSSPIESKR KNMLMADMPT AMLVRKEKRH PRGLTHISLN
IGDLKCHEID HIKILPPNPE GKVAEVLDAL HLKATDTLPW HRETARDFFS KYVDLDEPFK
TLSWCPGFDR MSSEQQELLR RAKARDVLTD GQMRRLIMDA IVESICKDMS SITPRLYSVA
SCPEHFRTDK VLEGGKGNVV DIMVKVNPGG RFSDTFLQQA RLGDTMRFSL ASPDVGKLIR
AHEPSAPLIA VSTGSGIGPV RAILQRRFVD SSRASGEFGR LGTSGALSRE PKRIEHAPVS
EHRSGRSSAH RRRNSLGGES RLPGTGRRAR LDARSARGSI SLFAGFKDVD SELIEHLVQP
AARAGLLDIV ELTPSNPEKK RVQDRMLLPE TRSRLAEKLK DPSCVVFVCA NEVAAEGVFA
NLSLIAGEDV KRLLGDRYVE EVFRD
//
