ID   NIA1_PHAVU              Reviewed;         881 AA.
AC   P39865;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=Nitrate reductase [NADH] 1;
DE            Short=NR-1;
DE            EC=1.7.1.1;
GN   Name=NIA1; Synonyms=NR1;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Saxa; TISSUE=Shoot;
RA   Hoff T., Stummann B.M., Henningsen K.W.;
RT   "Cloning and expression of a gene encoding a root specific nitrate
RT   reductase in bean (Phaseolus vulgaris).";
RL   Physiol. Plantarum 82:197-204(1991).
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; X53603; CAA37672.1; -; Genomic_DNA.
DR   PIR; S25445; S25445.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    881       Nitrate reductase [NADH] 1.
FT                                /FTId=PRO_0000166067.
FT   DOMAIN      515    590       Cytochrome b5 heme-binding.
FT   DOMAIN      625    737       FAD-binding FR-type.
FT   METAL       167    167       Molybdenum-pterin (Potential).
FT   METAL       221    221       Molybdenum-pterin (Potential).
FT   METAL       550    550       Iron (heme axial ligand) (By similarity).
FT   METAL       573    573       Iron (heme axial ligand) (By similarity).
FT   DISULFID    406    406       Interchain (Potential).
SQ   SEQUENCE   881 AA;  99223 MW;  A212A1288B4EE661 CRC64;
     MAASVEHRPF TSHQHGVVRS FKSYPDVPRP KKLPLPQPLS DSTNDNDEEA AVWKELVLKS
     SAGVEPSIFD PRDDGTSDQW IKRNASMIRL TGKHPFNAEP PLPRLMQHGF ITPSPIHYVR
     SHGPVPHARW EDWTVEVTGL VTRPTCFTME QLVNDFPSHE FPATLVCAGN RRKEQNMVKQ
     SIGFNWGAGG VSTSVWRGVS LRSLLKRCGI YSRAKGALHV CFEGAEDLPG GGGSNYGTSL
     MREVALDPSR DIILAYMQNG ELLSPDHGFP VRMIIPGFIG GRMVKWLKRI VVSNQQSQSH
     YHYKDNKLFP SHVDAELANE EDWWYKPEYI INEVNINSVI TTPSHQEILP INSWTTQMPY
     SMRGYAYSGG GRKVTRVEVT LDGGETWQVC SVERLEKPNK YGKYWCWCFW SLEVEVLDIL
     GAKEIAVRAW DEAQNTQPEK LIWNTMGMIN NCWFRVKTNV CKPKKGEIGI VFEHPTQPGN
     QSGGWMAREK QLEKSSESNP ILKKSVSSPF MNTATKSYSL SEVRRHNNRD SAWIIVNGHV
     YDCTRFLKDH PGGEDSILLN AGTDCTEEFE AIHSDKAKKM LEDYRIGELM TTDYTSDSSS
     SNNSVHGNSE TTHLAPIREV ALNPREKIPC KLLSKTSISH DVRLLRFALP AEDQVMGLPV
     GNHVFLCATV DEKLCMRAYT PTSSVDEVGF FDLVVKVYFK GVHPNFPNGG IMSQHLDSLP
     IGSVVDVKGP LGHIEYTGRG NFLVHGKPRF AKRLTMLAGG TGITPIYQVV QAILKDPEDR
     TEMYVVYANR TEDDILLKEE LDEWAKKHDR LKVWYVLQAN IREGWEYSVG FITESILREH
     VPLASPDTLA LTCGPPPMIQ FAVQPNLEKL GYDIQNDLLV F
//