ID   NIA_BEABA      STANDARD;      PRT;   894 AA.
AC   P43100;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Nitrate reductase [NADPH] (EC 1.7.1.3) (NR).
GN   Name=NIA;
OS   Beauveria bassiana (Tritirachium shiotae).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Cordyceps.
OX   NCBI_TaxID=176275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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: Requires FAD, a heme group (called cytochrome b-557) and
CC       one molybdenum atom.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X84950; CAA59336.1; -.
DR   PIR; S52857; S52857.
DR   HSSP; P04166; 1EUE.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR008335; Euk_Mb_oxred.
DR   InterPro; IPR008333; FAD_binding_6.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR005066; Mo-co_dimer.
DR   InterPro; IPR000572; Oxidored_molyb.
DR   InterPro; IPR001433; Oxred_FAD/NAD(P).
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   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; PS00559; MOLYBDOPTERIN_EUK; 1.
KW   FAD; Flavoprotein; Heme; Molybdenum; NADP; Nitrate assimilation;
KW   Oxidoreductase.
FT   METAL       169    169       Molybdenum-pterin (Potential).
FT   METAL       220    220       Molybdenum-pterin (Potential).
FT   DISULFID    418    418       Interchain (Potential).
FT   METAL       570    570       Iron (heme axial ligand) (By similarity).
FT   METAL       593    593       Iron (heme axial ligand) (By similarity).
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
//