ID   NIA_PHYIN               Reviewed;         902 AA.
AC   P39864;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 62.
DE   RecName: Full=Nitrate reductase [NADPH];
DE            Short=NR;
DE            EC=1.7.1.3;
GN   Name=NIAA;
OS   Phytophthora infestans (Potato late blight fungus).
OC   Eukaryota; stramenopiles; Oomycetes; Peronosporales; Phytophthora.
OX   NCBI_TaxID=4787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 88069;
RX   MEDLINE=95339410; PubMed=7614559; DOI=10.1007/BF00352105;
RA   Pieterse C.M.J., van 't Klooster J., van den Berg-Velthuis G.C.M.,
RA   Govers F.;
RT   "NiaA, the structural nitrate reductase gene of Phytophthora
RT   infestans: isolation, characterization and expression analysis in
RT   Aspergillus nidulans.";
RL   Curr. Genet. 27:359-366(1995).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first
CC       step of nitrate assimilation in plants, fungi and bacteria.
CC   -!- CATALYTIC ACTIVITY: Nitrite + NADP(+) + H(2)O = nitrate + NADPH.
CC   -!- COFACTOR: Binds 1 FAD.
CC   -!- COFACTOR: Binds 1 heme group. The heme group is called cytochrome
CC       b-557.
CC   -!- COFACTOR: Binds 1 molybdenum ion.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; U14405; AAA86681.1; -; Genomic_DNA.
DR   PIR; S57199; S57199.
DR   HSSP; P04166; 1EUE.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR012137; Nitr_rd_NADH.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Gene3D; G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
DR   Gene3D; G3DSA:3.90.420.10; Oxred_molyb_bd; 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   ProDom; PD000612; Cyt_B5; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NADP;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    902       Nitrate reductase [NADPH].
FT                                /FTId=PRO_0000166047.
FT   DOMAIN      537    612       Cytochrome b5 heme-binding.
FT   DOMAIN      637    751       FAD-binding FR-type.
FT   NP_BIND     872    879       NADP (By similarity).
FT   METAL       182    182       Molybdenum-pterin (Potential).
FT   METAL       234    234       Molybdenum-pterin (Potential).
FT   METAL       572    572       Iron (heme axial ligand) (By similarity).
FT   METAL       595    595       Iron (heme axial ligand) (By similarity).
FT   DISULFID    419    419       Interchain (Potential).
SQ   SEQUENCE   902 AA;  101074 MW;  05B9F4E1A381BBE6 CRC64;
     MTRLRSAAST ITNRSTPALA LTASHAGSHP AVIVPIQPLL LTLERRPSCP HRVSYPEIEA
     YRGISSSLRS HNAIVRASDI MAQIDPRDVG TPDEWVPRHP ELIRLTGRHP FNSEPPLKYA
     STFITPMALH YVRNHGPVPR LEWDTHTFSI DGLVKKPRTF GMNELVTTFE QETVTFPVLL
     VCAGNRRKEQ NMIKKTIGFS WGAAGCSTAE WTGVPLHVLL TACGVDREKA QWVWFEGIED
     LPHDKYGTCI RASTELDPEC DVLVAWKANG ELLGPDHGFP VRLIVPGHIG GRMVKWLERI
     HVSDHESSNH HHIMDNRVLP SHVTAETATA EGWWSKSPYA IMELNVNAVV ILPNHDDLLA
     LGEDTTFNDI ETYTIKGYAY SGGGRRVIRV EVTLDDGASW QLARIIYHER PSKYGKMWCW
     VHYELAAPMS SLLCAREVCV RAWDSSMNLM PAFPTWNVMG MMNNPWYRVK IHHEQDTNSL
     RFEHPTQAGN QKGGWMTKER IMTNDVDSIK MLQVEPLDTS SAATPKPGLT ADELSELPLI
     FADEVAKHNS KKSCWFICRD LVYDATPFLD EHPGGATSIL LCGGTDCTDE FESIHSTKAW
     QMLKKYCIGR CSSTEDDTGT SDTSSDHEET DVALKGRTKV PIVLISREVV SHDARIFKFA
     LPAKDLRLGL PIGNHVFLYA KINGKTAVRA YTPISSENDE DRGFVSFLIK VYFAGDNPVH
     PEGGLFSQYL DGLHLGQQIQ IKGPLGHFTY YGDGNFSLET TNFHAYKFGF VAGGTGITPV
     YQVMRAILED AKDQTKVALI YCVRSQRDLL LRKELETLQK LRPGQCRIFY TLSDMELLDR
     NDPIVRGWAY GKSRLNFAMV KNIIGSDAED VCMCGPEGMI EYACKPALLK LNYDLKTQTT
     VF
//