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Database: UniProt
Entry: P27969
LinkDB: P27969
Original site: P27969 
ID   NIA2_HORVU              Reviewed;         912 AA.
AC   P27969;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   26-NOV-2014, entry version 91.
DE   RecName: Full=Nitrate reductase [NADH];
DE            Short=NR;
DE            EC=1.7.1.1;
DE   Flags: Fragment;
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 [MRNA].
RC   STRAIN=cv. Steptoe; TISSUE=Leaf;
RX   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:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00279}.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00716}.
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DR   EMBL; X57844; CAA40975.1; -; mRNA.
DR   PIR; S17454; RDBHNS.
DR   ProteinModelPortal; P27969; -.
DR   SMR; P27969; 653-912.
DR   Gramene; P27969; -.
DR   Genevestigator; P27969; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.650; -; 1.
DR   Gene3D; 3.10.120.10; -; 1.
DR   Gene3D; 3.90.420.10; -; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR014756; Ig_E-set.
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_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR   InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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   SUPFAM; SSF55856; SSF55856; 1.
DR   SUPFAM; SSF56524; SSF56524; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   SUPFAM; SSF81296; SSF81296; 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   Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW   Molybdenum; NAD; Nitrate assimilation; Oxidoreductase.
FT   CHAIN        <1    912       Nitrate reductase [NADH].
FT                                /FTId=PRO_0000166057.
FT   DOMAIN      535    610       Cytochrome b5 heme-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   DOMAIN      651    764       FAD-binding FR-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00716}.
FT   METAL       186    186       Molybdenum. {ECO:0000250}.
FT   METAL       570    570       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   METAL       593    593       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   DISULFID    425    425       Interchain. {ECO:0000255}.
FT   NON_TER       1      1
SQ   SEQUENCE   912 AA;  101467 MW;  47AB9C5B303190CC CRC64;
     SVEPRQPFGR LDAPATAPTA RAPGSNGIRR RADSPVRGCG FPSLISPPRK GPVAEEDEED
     DDEDDEGHED WREAYGSHLQ LEVEPSTRDP RDEGTADAWI ERNPSLIRLT GKHPLNCEPP
     LARLMHHGFI TPAPLHYVRN HGAVPRGDWA TWTVEVTGLV RRPARLTMDE LANGFPAAEV
     PATLVCAGNR RKEQNMVQQT VGFNWGAAGV STSVWRGARL RDVLLRCGVM SKKGQALNVC
     FEGAEDLPGG GGSKYGTSMS REWAMDPSRD IILPYAQNGE PLLPDHGYPV RVLIPGCIGG
     RMVKWVRRIV VTTAESDNYY HFKDNRVLPS HVDAELANAE AWWYRPEYII NELNTNSVIT
     TPGHDEILPI NAFTTQRAYT IKGYAYSGGG KKITRVEVTL DGGESWMLCT LDIPEKPNKY
     GRYWCWCFWS VEIEVLDLLG AKEVAVRAWD QTHNTQPEKL IWNLMGMMNN CWFKIKVNVC
     RPHKGEIGLV FEHPTQPGNQ TGGWMARQKH LETAEAAAPG LKRSTSTPFM NTAGDKQFTM
     SEVRKHGSKE SAWIVVHGHV YDCTAFLKDH PGGADSILIN AGSDCTEEFD AIHSDKAKAL
     LDTYRIGELI TTGTGYNSDN SVHGGSSLSH LAPIREATKV AGAPIALSSP REKVPCRLVD
     KKELSHDVRL FRFALPSSDQ VLGLPVGKHI FVCATIDGKL CMRAYTPTSM VDEIGQFELL
     VKVYFRDEHP KFPNGGLMTQ YLESLQVGSS SIDVKGPLGH VEYTGRGNFV INGKQRRARR
     LAMICGSSGI TPMYQVIQAV LRDQPEDETE MHLVYANRSE DDILLRDELD RWATEYPDRL
     KVWYVIDQVK RPEDGWKFSV GFVTEDILRA HVPEGGDDTL ALACGPPPMI KFAISPNLEK
     MKYDMANSFI SF
//
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