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Database: UniProt
Entry: W2FY22_PHYPR
LinkDB: W2FY22_PHYPR
Original site: W2FY22_PHYPR 
ID   W2FY22_PHYPR            Unreviewed;       827 AA.
AC   W2FY22;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Nitrate reductase [NADPH] {ECO:0000313|EMBL:ETK75662.1};
GN   ORFNames=L915_17767 {ECO:0000313|EMBL:ETK75662.1}, L916_17668
GN   {ECO:0000313|EMBL:ETL29092.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK75662.1};
RN   [1] {ECO:0000313|EMBL:ETK75662.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK75662.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETL29092.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL29092.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC       of nitrate assimilation in plants, fungi and bacteria.
CC       {ECO:0000256|ARBA:ARBA00003838}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000233-1};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000233-1};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC       {ECO:0000256|ARBA:ARBA00006253}.
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DR   EMBL; KI688774; ETK75662.1; -; Genomic_DNA.
DR   EMBL; KI675569; ETL29092.1; -; Genomic_DNA.
DR   EnsemblProtists; ETK75662; ETK75662; L915_17767.
DR   EnsemblProtists; ETL29092; ETL29092; L916_17668.
DR   VEuPathDB; FungiDB:PPTG_16901; -.
DR   Proteomes; UP000053236; Unassembled WGS sequence.
DR   Proteomes; UP000053864; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   CDD; cd02112; eukary_NR_Moco; 1.
DR   Gene3D; 2.60.40.650; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR012137; Nitr_rd_NADH.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR   InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF03404; Mo-co_dimer; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00174; Oxidored_molyb; 1.
DR   PIRSF; PIRSF000233; Nitr_rd_NADH; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00407; EUMOPTERIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000233-1};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000233-
KW   1}; Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          459..534
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          562..676
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         102
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000233-1"
SQ   SEQUENCE   827 AA;  92613 MW;  5EB7C310E510D2C6 CRC64;
     MAQIDPRDVG TPDEWVPRHP ELIRLTGRHP FNSEPPLKYT STFITPMALH YVRNHGPVPR
     LDWNTHTFSI DGLVNKPRTF GMDELVTTFV KETVTFPVLL VCAGNRRKEQ NMIKKTIGFS
     WGAAGCSTAE WTGVPLHVLL TACGVDREKA QWVWFEGIED LPHDKYGTCI RASTALDPAC
     DVLVAWKANG ELLTPDHGFP IRLIIPGHIG GRMVKWLARI HVSDQESTNH HHIMDNRVLP
     SHVTAETATA EGWWSKSPYA IMELNVNAAI IKPNHDDLLA LSEDDTVNDI ETYTIKGYAY
     SGGGRRVIRV EVTLDDGATW QLAHIIYHER PSKYGKMWCW VHYELAVQVS SLLRAREVCA
     RAWDSSMNLM PEFPTWNVMG MMNNPWYRVK IHHEQGTNTL RFEHPTQAGN QKGGWMTKER
     IMTNDNEPIR GKKLQVELID TSSDATPKPG LTADEFSELP LISAEEVAKH NTNESCWFIC
     RGLVYDATPF LDEHPGGATS ILLCGGTDCT DEFESIHSTK AWLMLKKYCI GRCPSTDDDT
     GTSDTASSSA DQEETDVALK GATKVPVVLI SREVVSHDAR IFKFALPAKD LRLGLPVGNH
     VFLYANINGK TIVRAYTPIS SESDEDRGFV SFLIKVYFAG DNPVHPEGGL FSQYLDGLHL
     GQQIQIKGPL GHFTYHGEGS FSLESTNFHV NKFGFIAGGT GITPVYQVMR AILENAKDQT
     KVALIYCVRS ERDLLLRKEL ETLQKLRPSQ CRIFYTLSDL EQLDKNDPIV RGWAYGKSRL
     NFAMVKNIIG SDADHVGMCG PEGMIEYACK PALLKLNYDL KTQTTVF
//
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