ID   NIA1_HORVU              Reviewed;         915 AA.
AC   P27967;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Nitrate reductase [NADH];
DE            Short=NR;
DE            EC=1.7.1.1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Himalaya; TISSUE=Leaf;
RX   MEDLINE=91326031; PubMed=1865878; DOI=10.1007/BF00273931;
RA   Schnorr K.M., Juricek M., Huang C., Culley D., Kleinhofs A.;
RT   "Analysis of barley nitrate reductase cDNA and genomic clones.";
RL   Mol. Gen. Genet. 227:411-416(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 per subunit.
CC   -!- COFACTOR: Binds 1 heme group per subunit.
CC   -!- COFACTOR: Binds 1 molybdenum-pterin group per subunit.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X57845; CAA40976.1; -; Genomic_DNA.
DR   PIR; S17453; RDBHNH.
DR   HSSP; P17571; 2CND.
DR   SMR; P27967; 656-915.
DR   Gramene; P27967; -.
DR   BRENDA; 1.7.1.1; 283.
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   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW   Molybdenum; NAD; Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    915       Nitrate reductase [NADH].
FT                                /FTId=PRO_0000166056.
FT   DOMAIN      538    613       Cytochrome b5 heme-binding.
FT   DOMAIN      654    767       FAD-binding FR-type.
FT   METAL       189    189       Molybdenum-pterin (Potential).
FT   METAL       243    243       Molybdenum-pterin (Potential).
FT   METAL       573    573       Iron (heme axial ligand) (By similarity).
FT   METAL       596    596       Iron (heme axial ligand) (By similarity).
FT   DISULFID    428    428       Interchain (Potential).
SQ   SEQUENCE   915 AA;  101770 MW;  937FFA96B6FDAA56 CRC64;
     MAASVEPRQP FGRLDAPATA PTARAPGSNG IRRRADSPVR GCGFPSLISP PRKGPVAEEE
     EDDDDEDDEG HEDWREAYGS HLQLEVEPST RDPRDEGTAD AWIERNPSLI RLTGKHPLNC
     EPPLARLMHH GFITPAPLHY VRNHGAVPRG DWATWTVEVT GLVRRPARLT MDELANGFPA
     AEVPATLVCA GNRRKEQNMV QQTVGFNWGA AGVSTSVWRG ARLRDVLLRC GVMSKKGQAL
     NVCFEGAEDL PGGGGSKYGT SVSREWAMDP SRDIILPYAQ NGEPLLPDHG YPVRVLIPGC
     IGGRMVKWVR RIVVTTAESD NYYHFKDNRV LPSHVDAELA NAEAWWYRPE YIINELNTNC
     VITTPGHDEI LPINAFTTQR AYTIKGYAYS GGGKKITRVE VTLDGGESWM LCTLDIPEKP
     NKYGRYWCWC FWSVEIEVLD LLGAKEVAVR TWDQTHNTQP EKLIWNLMGM MNNCWFKIKV
     NVCRPHKGEI GLVFEHPTQP GNQTGGWMAR QKHLETAEAA APGLKRSTST PFMNTAGDKQ
     FTMSEVRKHG SKESAWIVVH GHVYDCTAFL KDHPGGADSI LINAGSDCTE EFDAIHSDKA
     KALLDTYRIG ELITTGTGYN SDNSVHGGSS LSHLAPIREA TKVAGAPIAL SSPREKVPCR
     LVDKKELSHD VRLFRFALPS SDQVLGLPVG KHIFVCATID GKLCMRAYTP TSMVDEIGQF
     ELLVKVYFRD EHPKFPNGGL MTQYLESLQV GSSYIDVKGP LGHVEYTGRG NFVINGKQRR
     ARRLAMICGG SGITPMYQVI QAVLRDQPED ETEMHLVYAN RSEDDILLRD ELDRWAAEYP
     DRLKVWYVID QVKRPEDGWK FSVGFVTEDI LRAHVPEGGD DTLALACGPP PMIKFAISPN
     LEKMKYDMAN SFISF
//