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 01-MAY-2013, entry version 131.
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; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
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.
CC -!- COFACTOR: Binds 1 heme group per subunit.
CC -!- COFACTOR: Binds 1 molybdenum-pterin group per subunit.
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 IPI; IPI00518959; -.
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; 118-490, 549-604, 662-917.
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 OMA; HGAVPKA; -.
DR PhylomeDB; P11832; -.
DR ProtClustDB; PLN02252; -.
DR BioCyc; MetaCyc:AT1G77760-MONOMER; -.
DR ArrayExpress; P11832; -.
DR Genevestigator; P11832; -.
DR GermOnline; AT1G77760; Arabidopsis thaliana.
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: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; 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 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; Phosphoprotein;
KW 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-pterin (Potential).
FT METAL 251 251 Molybdenum-pterin (Potential).
FT METAL 580 580 Iron (heme axial ligand) (By similarity).
FT METAL 603 603 Iron (heme axial ligand) (By similarity).
FT MOD_RES 69 69 Phosphoserine.
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
//
