ID   NIA1_BRANA              Reviewed;         911 AA.
AC   P39867;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=Nitrate reductase [NADH], clone PBNBR1405;
DE            Short=NR;
DE            EC=1.7.1.1;
GN   Name=NIA1;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lisandra;
RX   MEDLINE=96222419; PubMed=8685274; DOI=10.1104/pp.111.1.39;
RA   Fukuoka H., Ogawa T., Minami H., Yano H., Ohkawa Y.;
RT   "Developmental stage-specific and nitrate-independent regulation of
RT   nitrate reductase gene expression in rapeseed.";
RL   Plant Physiol. 111:39-47(1996).
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.
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; D38219; BAA07394.1; -; mRNA.
DR   PIR; T08105; T08105.
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    911       Nitrate reductase [NADH], clone
FT                                PBNBR1405.
FT                                /FTId=PRO_0000166051.
FT   DOMAIN      539    614       Cytochrome b5 heme-binding.
FT   DOMAIN      654    766       FAD-binding FR-type.
FT   METAL       191    191       Molybdenum-pterin (Potential).
FT   METAL       245    245       Molybdenum-pterin (Potential).
FT   METAL       574    574       Iron (heme axial ligand) (By similarity).
FT   METAL       597    597       Iron (heme axial ligand) (By similarity).
FT   DISULFID    430    430       Interchain (Potential).
SQ   SEQUENCE   911 AA;  102252 MW;  BBA4E19835B03D8C CRC64;
     MATSVDNRHY PRLSSALNGG VVHSFKPPLV PSPSLDRDQD QSVNVPTEKS VDKTTKEDRF
     DSSDDEDESH NRYVSYYKEM VLKSNSDLEP TALDSRDEST GDKWIHRNSS MVRLTGKHPF
     NAEAPLPRLM HHGFITPVPL HYVRNHGGVP KAEWSDWSVE VTGLVKRPAG LTMEQLISEF
     PSREFPVTLV CAGNRRKEQN MVKQTIGFNW GSAGVSTSLW RGVALSDVLR RCGVYSKRGG
     ALNVCFEGAE DLPGGGGSKY GTSIKKEMAM DPARDIILAY MQNGELLTPD HGFPVRVIIP
     GFIGGRMVKW LKRIIVTPQE SDNYYHYKDN RVLPSYVDAE LPNEESWWYR PEYIINELNI
     NSVITTPGHE EILPINAFTT QKPYTLKGYA YSGGGKKVTR VEVTLDGGET WSVCELDHQE
     KPNKYGKFWC WCFWSLDVEV LDLLSAKEVA VRAWDESLNT QPEKLIWNLM GMMNNCWFRI
     KTNVCKPHRG EIGIVFEHPT RPGNQSGGWM AKERQIEKSS ESHPTLKKSV STPFMNTASK
     MYSMSEVRKH NSAESAWIIV HGHIYDCTRF LKDHPGGSDS ILINAGTDCT EEFEAIHSDK
     AKKLLEDYRI GELITTGYDS SPNVSVHGGS SVMSLLAPIR QLAPTKNIAL VNPREKVPVK
     LIEKTSISHD VRRFRFALPS EDQQLGLPVG KHIFLCATIN DKLCLRAYTP TSTVDAVGYI
     DLVIKVYFKN VHPRFPNGGL MSQHPDSLPI GAVLDIKGPL GHIEYQGRGK FMVSGKPKFA
     NKLAMLAGGT GITPIYQVIQ SILSDPEDET EMFVVYANRT EDDILVREEL EGWASKFPDR
     LKIWYVVEIA KEGWEYSTGF ITEAVLREHV PEGLEGESLA LACGPPPMIQ FALQPNLEKM
     GYDIKEDLLI F
//