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Database: UniProt
Entry: P27783
LinkDB: P27783
Original site: P27783 
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   26-NOV-2014, entry version 89.
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; Gunneridae;
OC   Pentapetalae; 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:
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   -!- INDUCTION: By nitrate.
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; 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: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; 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                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   DOMAIN      642    754       FAD-binding FR-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00716}.
FT   METAL       180    180       Molybdenum. {ECO:0000250}.
FT   METAL       563    563       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   METAL       586    586       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   DISULFID    419    419       Interchain. {ECO:0000255}.
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
//
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