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Database: UniProt
Entry: P11832
LinkDB: P11832
Original site: P11832 
ID   NIA1_ARATH              Reviewed;         917 AA.
AC   P11832; Q9CA18;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 3.
DT   19-MAR-2014, entry version 138.
DE   RecName: Full=Nitrate reductase [NADH] 1;
DE            Short=NR1;
DE            EC=1.7.1.1;
GN   Name=NIA1; OrderedLocusNames=At1g77760; ORFNames=T32E8.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT THR-198, AND HERBICIDE
RP   RESISTANCE.
RC   STRAIN=cv. Columbia;
RX   PubMed=8510658;
RA   Wilkinson J.Q., Crawford N.M.;
RT   "Identification and characterization of a chlorate-resistant mutant of
RT   Arabidopsis thaliana with mutations in both nitrate reductase
RT   structural genes NIA1 and NIA2.";
RL   Mol. Gen. Genet. 239:289-297(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 342-360 AND 525-917.
RX   PubMed=2905260;
RA   Cheng C., Dewdney J., Nam H., den Boer B.G.W., Goodman H.M.;
RT   "A new locus (NIA 1) in Arabidopsis thaliana encoding nitrate
RT   reductase.";
RL   EMBO J. 7:3309-3314(1988).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
RA   Andreasson E., Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from
RT   Arabidopsis thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
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 (By similarity).
CC   -!- COFACTOR: Binds 1 heme group per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per
CC       subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Root, leaf, and shoot.
CC   -!- MISCELLANEOUS: When mutated confers resistance to the herbicide
CC       chlorate.
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; Z19050; CAA79494.1; -; Genomic_DNA.
DR   EMBL; AC012193; AAG51627.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36018.1; -; Genomic_DNA.
DR   EMBL; AY090950; AAM13997.1; -; mRNA.
DR   EMBL; AF424624; AAL11617.1; -; mRNA.
DR   EMBL; BT000989; AAN41389.1; -; mRNA.
DR   EMBL; X13434; CAA31786.1; -; mRNA.
DR   EMBL; X13436; CAA31788.1; -; Genomic_DNA.
DR   PIR; E96807; E96807.
DR   PIR; S35228; S35228.
DR   RefSeq; NP_177899.1; NM_106425.2.
DR   UniGene; At.17771; -.
DR   ProteinModelPortal; P11832; -.
DR   SMR; P11832; 95-533, 549-604, 662-917.
DR   BioGrid; 29331; 7.
DR   IntAct; P11832; 4.
DR   STRING; 3702.AT1G77760.1-P; -.
DR   PaxDb; P11832; -.
DR   PRIDE; P11832; -.
DR   EnsemblPlants; AT1G77760.1; AT1G77760.1; AT1G77760.
DR   GeneID; 844112; -.
DR   KEGG; ath:AT1G77760; -.
DR   TAIR; AT1G77760; -.
DR   eggNOG; COG0543; -.
DR   HOGENOM; HOG000252609; -.
DR   InParanoid; P11832; -.
DR   KO; K10534; -.
DR   OMA; FHIGTLV; -.
DR   PhylomeDB; P11832; -.
DR   ProtClustDB; PLN02252; -.
DR   BioCyc; MetaCyc:AT1G77760-MONOMER; -.
DR   ArrayExpress; P11832; -.
DR   Genevestigator; P11832; -.
DR   GO; GO:0005829; C:cytosol; TAS:TAIR.
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:0008940; F:nitrate reductase activity; IMP:TAIR.
DR   GO; GO:0042128; P:nitrate assimilation; IMP:TAIR.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:TAIR.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
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   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; FAD; Flavoprotein; Heme;
KW   Herbicide resistance; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase; Reference proteome.
FT   CHAIN         1    917       Nitrate reductase [NADH] 1.
FT                                /FTId=PRO_0000166049.
FT   DOMAIN      545    620       Cytochrome b5 heme-binding.
FT   DOMAIN      660    772       FAD-binding FR-type.
FT   METAL       197    197       Molybdenum (By similarity).
FT   METAL       580    580       Iron (heme axial ligand) (By similarity).
FT   METAL       603    603       Iron (heme axial ligand) (By similarity).
FT   DISULFID    436    436       Interchain (Potential).
FT   MUTAGEN     198    198       A->T: Loss of activity.
FT   CONFLICT     17     17       A -> R (in Ref. 1; CAA79494).
SQ   SEQUENCE   917 AA;  103041 MW;  6FD3ED46B9F63825 CRC64;
     MATSVDNRHY PTMNGVAHAF KPPLVPSPRS FDRHRHQNQT LDVILTETKI VKETEVITTV
     VDSYDDSSSD DEDESHNRNV PYYKELVKKS NSDLEPSILD PRDESTADSW IQRNSSMLRL
     TGKHPFNAEA PLPRLMHHGF ITPVPLHYVR NHGAVPKANW SDWSIEITGL VKRPAKFTME
     ELISEFPSRE FPVTLVCAGN RRKEQNMVKQ TIGFNWGSAG VSTSLWKGIP LSEILRRCGI
     YSRRGGALNV CFEGAEDLPG GGGSKYGTSI KKEMAMDPAR DIILAYMQNG ELLTPDHGFP
     VRVIVPGFIG GRMVKWLKRI IVTPQESDSY YHYKDNRVLP SLVDAELANS EAWWYKPEYI
     INELNINSVI TTPGHAEILP INAFTTQKPY TLKGYAYSGG GKKVTRVEVT LDGGDTWSVC
     ELDHQEKPNK YGKFWCWCFW SLDVEVLDLL SAKDVAVRAW DESFNTQPDK LIWNLMGMMN
     NCWFRIRTNV CKPHRGEIGI VFEHPTRPGN QSGGWMAKER QLEISSESNN TLKKSVSSPF
     MNTASKMYSI SEVRKHNTAD SAWIIVHGHI YDCTRFLKDH PGGTDSILIN AGTDCTEEFE
     AIHSDKAKKL LEDYRIGELI TTGYDSSPNV SVHGASNFGP LLAPIKELTP QKNIALVNPR
     EKIPVRLIEK TSISHDVRKF RFALPSEDQQ LGLPVGKHVF VCANINDKLC LRAYTPTSAI
     DAVGHIDLVV KVYFKDVHPR FPNGGLMSQH LDSLPIGSMI DIKGPLGHIE YKGKGNFLVS
     GKPKFAKKLA MLAGGTGITP IYQIIQSILS DPEDETEMYV VYANRTEDDI LVREELEGWA
     SKHKERLKIW YVVEIAKEGW SYSTGFITEA VLREHIPEGL EGESLALACG PPPMIQFALQ
     PNLEKMGYNV KEDLLIF
//
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