ID   NIA_BEABA               Reviewed;         894 AA.
AC   P43100;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Nitrate reductase [NADPH];
DE            Short=NR;
DE            EC=1.7.1.3;
GN   Name=NIA;
OS   Beauveria bassiana (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=176275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB147;
RA   Maurer P.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
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; X84950; CAA59336.1; -; Genomic_DNA.
DR   PIR; S52857; S52857.
DR   HSSP; P04166; 1EUE.
DR   BRENDA; 1.7.1.3; 97823.
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:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR001834; NADH-Cyt_B5_reductase.
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; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW   Molybdenum; NADP; Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    894       Nitrate reductase [NADPH].
FT                                /FTId=PRO_0000166041.
FT   DOMAIN      535    610       Cytochrome b5 heme-binding.
FT   DOMAIN      638    749       FAD-binding FR-type.
FT   METAL       169    169       Molybdenum-pterin (Potential).
FT   METAL       220    220       Molybdenum-pterin (Potential).
FT   METAL       570    570       Iron (heme axial ligand) (By similarity).
FT   METAL       593    593       Iron (heme axial ligand) (By similarity).
FT   DISULFID    418    418       Interchain (Potential).
SQ   SEQUENCE   894 AA;  99934 MW;  D0ED234BF1B1322B CRC64;
     MAVKSQLGVT YTTKTFPPSP PRTVGNSHAG SDDERDEVDA TPTTPPVEKL GQLLKPYSLP
     PTNTPTHVLP EDLKTPDHRV NRDPRLIRLT GVHPFNVEPP LTDLYDEGFL NSENLHYVRN
     HGPVPHCPDD ESLNWTFTVD GLVEKPFTIA VRDLIQKYDQ FTYPVTLVCA GNRRKEQNVV
     RKSKGFSWGA AGLSTALWTG VPIGALLRMA KPKRAAKYVC FEGADKLPNG YYGTSVKLNW
     CMDENRGIMV AHKMNGQSLH PDHGKPVRII IPGQIGGRSV KWLKKITITS EPSDNWYHIY
     DNRVLPTTIS PDASANLPDV WKDEKYAIYD LNANSAICYP RHDERLVLAT APDTYKVRGY
     AYGGGGKRIT RLEVTLNKGK SWLLAGIHYP EDDYRRAPDG DLLYGGSTDM WWRETCFCWC
     FWEIDIPVAD LSAADDIMIR AMDEGMMVQP RDMYWSVLGM MNNPWFRVVI HKEDGALRFE
     HPTQPALMPG GWMERVKRRG GNLTNGFWGE KTAAEEEQVL AEPEKEICMT NPKVVRIISL
     EELKAHEGEM EPWFVVNGHV YNGTPYLDNH PGGATSIINA AAQDATEEFM TIHSENAKAM
     MPQYHIGTLN DAARKALEGS AEESPASDPT RAVFLQPKYW SKAILETKTD VSSDSKIFSF
     RLDHAAQSIG LPTGQHLLVR LRDPATREAV IRAYTPLSET HAKGQLDILI KIYRDVPGQP
     GGKMTQALDS IPLGHFVDIK GPVGKFEYLG KGHCTVSGTS RHVRRFVMIC AGSGVTPIFQ
     VLRAVTSDAQ DGTECLVLDG NRCEKDILCR EELDAMVARA PARTTLLHKL SRPDASWCGL
     RGRMDKEYLE EHIGGFRKSD GREMVLVCGP AALEETVRSV LVEMAWKPED MLFF
//