ID NIA_BETPN Reviewed; 898 AA.
AC P27783;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-APR-2013, entry version 84.
DE RecName: Full=Nitrate reductase [NAD(P)H];
DE Short=NR;
DE EC=1.7.1.2;
GN Name=NIA1;
OS Betula pendula (European white birch) (Betula verrucosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Fagales; Betulaceae; Betula.
OX NCBI_TaxID=3505;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=1675424; DOI=10.1007/BF00260713;
RA Friemann A., Brinkmann K., Hachtel W.;
RT "Sequence of a cDNA encoding the bi-specific NAD(P)H-nitrate reductase
RT from the tree Betula pendula and identification of conserved protein
RT regions.";
RL Mol. Gen. Genet. 227:97-105(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(P)(+) + H(2)O = nitrate +
CC NAD(P)H.
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 -!- INDUCTION: By nitrate.
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; X54097; CAA38031.1; -; mRNA.
DR PIR; S15959; RDBJNH.
DR ProteinModelPortal; P27783; -.
DR SMR; P27783; 643-898.
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:0050463; F:nitrate reductase [NAD(P)H] 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; NADP; Nitrate assimilation; Oxidoreductase.
FT CHAIN 1 898 Nitrate reductase [NAD(P)H].
FT /FTId=PRO_0000166075.
FT DOMAIN 528 603 Cytochrome b5 heme-binding.
FT DOMAIN 642 754 FAD-binding FR-type.
FT METAL 180 180 Molybdenum-pterin (Potential).
FT METAL 234 234 Molybdenum-pterin (Potential).
FT METAL 563 563 Iron (heme axial ligand) (By similarity).
FT METAL 586 586 Iron (heme axial ligand) (By similarity).
FT DISULFID 419 419 Interchain (Potential).
SQ SEQUENCE 898 AA; 101002 MW; C6B2B2B12FBCDC58 CRC64;
MAASVENRRF THHEPAVNGL VRTFKPVPNS HRSDSPDLGR QIPSSPKKQV ATGEDSSSED
ENENDYKELI QKGNGELEPS ILDPRDEATA DNWVERNATM VRLTGKHPFN SEAPLTRLMH
HGFITPAPLH YVRNHGPVPK ARWEDWSVEV CGLVKRPARF TMDRLVTEFR SREFPVTLVC
AGNRRKEQNM VKKTIGFNWG AAGVSTSVWR GVPLRDVLKR CGIFSRGRGA FNVCFEGAED
LPGGGGSKYG TSVKYEMAMD PARDIILGYM QNGERLSPDH GFPVRMIIPG FIGGRMVKWL
KRIIVTTKES DNYYHYNDNR VLPSHVDADV AKAEAWWYKP EHIINELNIN SVITTPCHEE
ILPINSWTTQ RPYTLRGYAY SGGGRKVTRV EITMNGGEKW RVCALDHPEK PNKYGKYWCW
CFWSLEVEVL DLLGAKEIAV RAWDEAHNTQ PEKLIWNVMG MMNNCWFRVK TNVCKAHMGE
IGIAFEHPTV PGNESGGWMA REKNLETSSD ANQSLKKSVS SPFMNTSSKM FSMSEVKKHN
SAESAWIIVH GHIYDCTHFL KDHPGGADSI LINAGTDCTE EFDAIHSDKA KKMLEDYRIG
ELITTGYVSD SPNSTVHGAS NTSHLAPIKE IAPLRNVALI PGAKIPTKLV YKKSLSHDVR
LFRLALPSDD QVLGLPVGKH VFLCATIDDK LCMRAYTPTS TIDEVGYLDL VVKIYFKNSN
PRFPNGGLMS QHLDSLPIGS VLHVKGPLGH VEYTGRGNFL VHGEPKFAKR LAMVAGGTGI
TPIYQVIQAI LKDPEDETEM FVVYANRTED DILLREELDD WAKKHEKLKV WYVVKESKRE
GWEYSVGYIR ESILREHIPE GSDDVLALAC GAPSMIEEAV RLNLEKMNYD TKNSLIIF
//
