ID   NIA_PETHY               Reviewed;         909 AA.
AC   P36859;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=Nitrate reductase [NADH];
DE            Short=NR;
DE            EC=1.7.1.1;
GN   Name=NIA;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. TLRL13; TISSUE=Leaf;
RX   MEDLINE=93292981; PubMed=8514183; DOI=10.1016/0378-1119(93)90557-J;
RA   Salanoubat M., Ha D.B.D.;
RT   "Analysis of the petunia nitrate reductase apoenzyme-encoding gene: a
RT   first step for sequence modification analysis.";
RL   Gene 128:147-154(1993).
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 + NAD(+) + H(2)O = nitrate + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- COFACTOR: Binds 1 heme group per subunit.
CC   -!- COFACTOR: Binds 1 molybdenum-pterin group per subunit.
CC   -!- ENZYME REGULATION: Regulated by the nitrogen source and controlled
CC       by the circadian rhythm.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Maximum expression 2 hours after sunrise. Low
CC       expression found 2 hours before and 8 hours after sunrise.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L13691; AAA33713.1; -; Genomic_DNA.
DR   HSSP; P17571; 2CND.
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:0009703; F:nitrate reductase (NADH) 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; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    909       Nitrate reductase [NADH].
FT                                /FTId=PRO_0000166066.
FT   DOMAIN      535    610       Cytochrome b5 heme-binding.
FT   DOMAIN      652    764       FAD-binding FR-type.
FT   METAL       187    187       Molybdenum-pterin (Potential).
FT   METAL       241    241       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    426    426       Interchain (Potential).
SQ   SEQUENCE   909 AA;  102376 MW;  502C706F6E63E706 CRC64;
     MAASVENRQF SHLEPGLSGV VRSFKPRSDS PVRGCNFPLN NELTNFQKKP NTTIYLDCSS
     SEDDDDDDDK NEYLQMIRKG KLEVEPSVHD IRDEGTADNW IERNNSMIRL TGKHPFNSEP
     PLARLMHHGF ITPVPLHYVR NHGPVPKGMW DDWTVEVTGL VKRPMKFTME QLVNEFPSRE
     LPVTLVCAGN RRKEQNMVKQ TIGFNWGAAA VSTTVWRGVP LRAILKRCGI YSRTKGALNI
     CFEGADVLPG GGGSKYGTSI KKEFAMDPSR DIIIAYMQNG EKLTPDHGFP LRMIIPGFIG
     GRMVKWLKRI IVTTQESESY YHYKDNRVLP PHVDAELANA EAWWYKPEYI INELNINSVI
     TTPCHEEILP INSWTTQRPY TLRGYSYSGG GKKVTRVEVT MDGGETWNVC TVDHPEKPNK
     YGKYWCWCFW SLEVEVLDLL SAKEIAVRAW DETLNTQPEK LIWNVMGMMN NCWFRVKTNV
     CKPHKGEIGI VFEHPTQPGN LSGGWMAKER HLEISAEAPP TLKKSISTPF MNTASKMYSM
     SEVKKHNSAD SAWIIVHGHV YDATRFLKDH PGGIDSILIN AGTDCTEEFD AIHSDKAKKL
     LEDFRIGELI TTGYTSDSSP NNSVHGSSSF SGFLAPIKEL APAVRSVALI PREKIPCKLV
     DKKSISHDVR KFRFALPSED QVLGLPVGKH IFLCAIIDDK LCMRAYTPTS TVDEVGYFEL
     VVKIYFKGIV PKFPNGGQMS QYLDSLPLGA FVDVKGPLGH IEYQGRGNFL VHGKRKFAKK
     LAMLAGGTGI TPVYQVMQAI LKDPEDETEM HVVYANRTED DILLKDELDS WAVKLPERVK
     VWYVVQDSIK EGWKYSTGFI TEAVLREHIP LPSQTTLALA CGPPPMIQFA VNPNLEKMGY
     DIKDSLLVF
//