ID   NIA2_SOYBN              Reviewed;         890 AA.
AC   P39870;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 66.
DE   RecName: Full=Inducible nitrate reductase [NADH] 2;
DE            Short=NR;
DE            EC=1.7.1.1;
GN   Name=INR2;
OS   Glycine max (Soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Glycine.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Williams;
RX   MEDLINE=96123229; PubMed=8534848; DOI=10.1007/BF00020980;
RA   Wu S., Lu Q., Kriz A.L., Harper J.E.;
RT   "Identification of cDNA clones corresponding to two inducible nitrate
RT   reductase genes in soybean: analysis in wild-type and nr1 mutant.";
RL   Plant Mol. Biol. 29:491-506(1995).
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; U13987; AAA96813.1; -; mRNA.
DR   PIR; S66308; S66308.
DR   UniGene; Gma.8416; -.
DR   HSSP; P17571; 2CND.
DR   SMR; P39870; 636-890.
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    890       Inducible nitrate reductase [NADH] 2.
FT                                /FTId=PRO_0000166070.
FT   DOMAIN      517    592       Cytochrome b5 heme-binding.
FT   DOMAIN      634    746       FAD-binding FR-type.
FT   METAL       169    169       Molybdenum-pterin (Potential).
FT   METAL       223    223       Molybdenum-pterin (Potential).
FT   METAL       552    552       Iron (heme axial ligand) (By similarity).
FT   METAL       575    575       Iron (heme axial ligand) (By similarity).
FT   DISULFID    408    408       Interchain (Potential).
SQ   SEQUENCE   890 AA;  99945 MW;  3D1B373D9413F78C CRC64;
     MAASVDQRPY PGLHNGVVRP LKPGPDIPRP KKLPQAPPPL SDSSSDEEED TTLNLKDLIR
     KGTTEVESSI FDPRDDGTSD HWIQRNSSLV RLTGKHPFNS EPPLPRLMHH GFITPVPLHY
     VRNHGPVPRA RWEDWTVEVT GLVTRPTCFT MEQLLHDFPS REFPATLVCA GNRRKEQNMV
     KQSIGFNWGA AAISTSVWRG VPLRTLLKSC GIYTRTKGAL HVCFEGAEDL PGGGGSKYGT
     SILREVALDP SRDIILAYMQ NGEPLSPDHG FPVRMIIPGF IGGRMVKWLK RIIVTTDQSQ
     NYYHYKDNRV LPSHVDAELA NAQAWWYKPD YIINELNINS VITTPCHEEI LPINSWTTQM
     PYFIRGYAYS GGGRKVTRVE VTLDGGETWQ VCTLDCPEKP NKYGKYWCWC LWSVEVEVLD
     LLGAREIAVR AWDEALNTQP EKLIWNVMGM MNNCWFRVKT NVCRPHKGEI GIVFEHPTQP
     GNQSGGWMAK EKHLEKSSES NPTLKKSVSS PFMNTTSKTY TMSEVRRHNN ADSAWIIVHG
     HVYDCTRFLK DHPGGTDSIL INAGTDCTEE FEAIHSDKAK QMLEDYRIGE LTTTCYNSDS
     SSSNPSVHGS SDTIPLTPIK EVITPMRSVA LNPREKIPCK LISKTSISHD VRLFRFALPS
     DDLLMGLPVG KHIFLCATVD EKLCMRAYTP TSSVHEVGYF DLVVKVYFKG VHPKFPTGGI
     MSQHLDSLPI GSVLDVKGPL GHIVYTGRGN FLVHGKPRFA TRLAMLAGGT GITPIYQVVR
     AILKDPEDCT EMHVVYANRT EDDILLKEEL DEWAKKYDRL KVWYVIQASI REGWEYSVGF
     ITESILTEHI PNASPDTLAL TCGPPPMIQF AVQPNLEKLG YDTQNNLLVF
//