ID   NIA2_TOBAC              Reviewed;         904 AA.
AC   P08509;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   16-JUN-2009, entry version 82.
DE   RecName: Full=Nitrate reductase [NADH] 2;
DE            Short=NR2;
DE            EC=1.7.1.1;
GN   Name=NIA2;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Xanthi; TISSUE=Leaf;
RA   Vaucheret H., Kronenberger J., Rouze P., Caboche M.;
RT   "Complete nucleotide sequence of the two homeologous tobacco nitrate
RT   reductase genes.";
RL   Plant Mol. Biol. 12:597-600(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 171-724.
RX   PubMed=17193712; DOI=10.1007/BF00331162;
RA   Calza R., Huttner E., Vincentz M., Rouze P., Galangau F.,
RA   Vaucheret H., Cherel I., Meyer C., Kronenberger J., Caboche M.;
RT   "Cloning of DNA fragments complementary to tobacco nitrate reductase
RT   mRNA and encoding epitopes common to the nitrate reductases from
RT   higher plants.";
RL   Mol. Gen. Genet. 209:552-562(1987).
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.
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; X14059; CAA32217.1; -; Genomic_DNA.
DR   EMBL; X06134; CAA29497.1; -; mRNA.
DR   PIR; S04839; RDNTNS.
DR   HSSP; P17571; 2CND.
DR   BRENDA; 1.7.1.1; 298.
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:0009703; F:nitrate reductase (NADH) 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   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW   Molybdenum; NAD; Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    904       Nitrate reductase [NADH] 2.
FT                                /FTId=PRO_0000166073.
FT   DOMAIN      531    606       Cytochrome b5 heme-binding.
FT   DOMAIN      647    759       FAD-binding FR-type.
FT   METAL       183    183       Molybdenum-pterin (Potential).
FT   METAL       237    237       Molybdenum-pterin (Potential).
FT   METAL       566    566       Iron (heme axial ligand) (By similarity).
FT   METAL       589    589       Iron (heme axial ligand) (By similarity).
FT   DISULFID    422    422       Interchain (Potential).
SQ   SEQUENCE   904 AA;  101958 MW;  75196875A3561D69 CRC64;
     MAASVENRQF SHLEAGLSRS FKPRSDSPVR GCNFPSPNST NFQKKPNSTI YLDYSSSEDD
     DDDDEKNEYL QMIKKGNSEL EPSVHDTRDE GTADNWIERN FSMIRLTGKH PFNSEPPLNR
     LMHHGFITPV PLHYVRNHGP VPKGTWDDWT VEVTGLVKRP MKFTMDQLVN EFPCRELPVT
     LVCAGNRRKE QNMVKQTIGF NWGAAAVSTT IWRGVPLRAL LKRCGVFSKN KGALNVCFEG
     ADVLPGGGGS KYGTSIKKEF AMDPARDIIV AYMQNGEKLA PDHGFPVRMI IPGFIGGRMV
     KWIKRIIVTT QESDSYYHFK DNRVLPPHVD AELANTEAWW YKPEYIINEL NINSVITTPC
     HEEILPINAW TTQRPYTLRG YSYSGGGKKV TRVEVTLDGG ETWQVSTLDH PEKPTKYGKY
     WCWCFWSLEV EVLDLLSAKE IAVRAWDETL NTQPEKLIWN VMGMMNNCWF RVKMNVCKPH
     KGEIGIVFEH PTQPGNQSGG WMAKERHLEI SAEAPQTLKK SISTPFMNTA SKMYSMSEVR
     KHSSADSAWI IVHGHIYDAT RFLKDHPGGT DSILINAGTD CTEEFDAIHS DKAKKLLEDF
     RIGELITTGY TSDSPGNSVH GSSSFSSFLA PIKELVPAQR SVALIPREKI PCKLIDKQSI
     SHDVRKFRFA LPSEDQVLGL PVGKHIFLCA VIDDKLCMRA YTPTSTIDEV GYFELVVKIY
     FKGIHPKFPN GGQMSQYLDS MPLGSFLDVK GPLGHIEYQG KGNFLVHGKQ KFAKKLAMIA
     GGTGITPVYQ VMQAILKDPE DDTEMYVVYA NRTEDDILLK EELDSWAEKI PERVKVWYVV
     QDSIKEGWKY SIGFITEAIL REHIPEPSHT TLALACGPPP MIQFAVNPNL EKMGYDIKDS
     LLVF
//