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 03-APR-2013, entry version 85.
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: 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; 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: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; Cyt_B5; 1.
DR SUPFAM; SSF81296; Ig_E-set; 1.
DR SUPFAM; SSF56524; Oxidored_molyb; 1.
DR SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 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 DOMAIN 651 764 FAD-binding FR-type.
FT METAL 186 186 Molybdenum-pterin (Potential).
FT METAL 240 240 Molybdenum-pterin (Potential).
FT METAL 570 570 Iron (heme axial ligand) (By similarity).
FT METAL 593 593 Iron (heme axial ligand) (By similarity).
FT DISULFID 425 425 Interchain (Potential).
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
//
