ID   NIA2_BRANA              Reviewed;         911 AA.
AC   P39868;
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 PBNBR1412;
DE            Short=NR;
DE            EC=1.7.1.1;
GN   Name=NIA2;
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; D38220; BAA07395.1; -; mRNA.
DR   PIR; T08108; T08108.
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                                PBNBR1412.
FT                                /FTId=PRO_0000166052.
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;  102201 MW;  BA06FEC14114DC21 CRC64;
     MATSVDNRHY PRLNPAINGV VRSFKPPPIP SPRHQNKTVS FLTEKVIVKE TKNDAVDDSY
     DSSDDEDESH NRNVSYYKEM IRKSHSDVEP SILDSRDEST ADNWIHRNSS MVRLTGKHPF
     NAEPPLPRLM HHGFITPVPL HYVRNHGTVP KADWSEWTVE ITGLVKRPAK FTMEELISEF
     PSREFPVTLV CAGNRRKEQN MVKQTIGFNW GSAGVSTSLW KGVPLSEILG RCGIYSRRGG
     GLNVCFEGAE DLPGGGGSKY GTSIKKEMAM DPARDIILAY MQNGELLTPD HGFPVRIIVP
     GFIGGRMVKW LKRIIVTPQE SDSYYHYKDN RVLPSLVDAE LANAEAWWYK PEYIINELNI
     NSVITTPGHQ EILPINAFTT QKPYTLKGYA YSGGGKKVTR VEVTLDGGDT WSVCDLDHQE
     KPNKYGKFWC WCFWSLDVEV LDLLSAKDVA VRAWDESFNT QPDKLIWNLM GMMNNCWFRI
     KTNVCKPHKG EIGIVFEHPT RPGNQSGGWM AKERQLEISS ESNPILKKSV SSPFMNTSAK
     MYSMSEVRKH NSVESAWIIV HGHIYDCTRF LKDHPGGSDS ILINAGTDCT EEFEAIHSDK
     AKKLLEDYRI GELITTGYDS SPNVSVHGGS TAVSLLAPIK ELAPSKNIAL VNPREKVPVT
     LIEKTSISHD VRRFRFALPS EDQQLGLPVG KHIFLCANIN DKLCLRAYTP TSTVDAVGHI
     DLVVKVYFKD VHPRFPNGGL MSQHLDSLPI GSVLNIKGPL GHIEYLGKGN FMVTGKPKFA
     KKLAMLAGGP GITPIYQVIQ SILSDPEDET EMFVVYANRT EDDILVREEL EGWANKHKDR
     LKVWYVVEIA KEGWNYSTGF ITEPVLREHV PEGLEGESLA LACGPPPMIQ FALQPNLEKM
     GYNVKEDLLI F
//