ID   A0A1X7RUZ1_ZYMTR        Unreviewed;      1126 AA.
AC   A0A1X7RUZ1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE            EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN   ORFNames=ZT3D7_G6348 {ECO:0000313|EMBL:SMQ51195.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ51195.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ51195.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT853696; SMQ51195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RUZ1; -.
DR   STRING; 1276538.A0A1X7RUZ1; -.
DR   Proteomes; UP000215127; Chromosome 5.
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:UP000215127}.
FT   DOMAIN          598..744
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          774..971
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1126 AA;  125563 MW;  6FA5B034B60A026C CRC64;
     MPSQEQESTA VCSSPRHIPK LAKPTPTRKH GDFTRHQQNE SNSSSSSDAE TEATDITSLS
     TSGTEVSEGL SAKEPSNDDD SPSVESVSFY DPARAIRCPA AQLELGKIAA AYPKLRPTGC
     TVDFCQSGRM IKTTEPRVGR DASIQEIQRD AQDFLCQLRA EDVIDSDERL QHRLNEVLVE
     IANTSCMSEQ HTASKRNDHH AAITSSIGGS WSQSLEELRH GLRLAWKHSS KCIMRSEYQT
     LEVRDFRHIN TSREMCTTVI AALREAFNNG KIAPTVFAFP PRQPGTRGPM FWNQQLLSFA
     AYEQDDGSVL GDPANLQLTK DITELGWCPP TFRTRWDLLP IVAMAEGDEP YWLEVAEKDF
     PLVPIAHPQL RLQFEKLGLR WVPAPALSRL GFDIGGVQYT AAPFIGWFMD AEIGVRNLAD
     TFRYNALPQV AVALNWIRSE HEIDRLPEYE RLAVLSRAQT ELNFAVYHSF KTAGVAMSDT
     LSASTMYCNY DDEHFRAKGF RLPSNPYWLA PPQGSIVPIW HRGGAPNYQP SPLICKHVQD
     PVNAWRRETR KSISEAAIKR IDKTDSPLAR SCSSASLQDH DVSHRQEASN DGVNQRRIYI
     CFCSAASTAK KLANDLHSRL RCVVDNQYAL NLVTTLNDFK PRKCSTEDIL LIVASTAGHG
     EVPLNGQRFL EVSFGAEAIS LLRYSIFGNG STLYGDRYNA AATAINEHLL NQKVKPLRDG
     LYTGDTAQEE PPWSQFDDWY RHIVEALHVE PDLLNQVTDR KQASKAKAGM ETASSYSLAR
     IVTCARSHAQ GIQHVVLDIG EQRYEPLSHV TMIVPNDSSV VKQALRTVGL KGNESAQVLH
     RHLSVEEYLV AFVDFDRPFL NLDWVQGWNF RRSQRHLFGR LPLREALQAF RWPWRTSIDL
     QSLLAAMPLK TPRMFSVASS QKVLKNGHHS GQLDLLIQHR EGGLVSNYLK TIGPGACVQL
     KTNPTEDETL LHSTDNPIIC FATGSGLAPV LSLLSHRLEL IKSSQQGSDG ENGRAFGAVT
     LILGFRKMDS SIIGQALREF IERGIIDVLL MTPSNDEKMR AQDRIFDCNV RQTLEKKLKC
     EGAAVFVCAL PEAAADFAKN LSAMLGCNVQ EALGERYVEQ VYKPAC
//