NIA1_ARATH
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 03-AUG-2022, entry version 190.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
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; DOI=10.1007/bf00281630;
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 structural
RT 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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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; DOI=10.1002/j.1460-2075.1988.tb03201.x;
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 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., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT 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 step
CC of nitrate assimilation in plants, fungi and bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate;
CC Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.1;
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; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
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. {ECO:0000305}.
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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_106425.3.
DR AlphaFoldDB; P11832; -.
DR SMR; P11832; -.
DR BioGRID; 29331; 8.
DR IntAct; P11832; 4.
DR STRING; 3702.AT1G77760.1; -.
DR iPTMnet; P11832; -.
DR PaxDb; P11832; -.
DR PRIDE; P11832; -.
DR ProteomicsDB; 251150; -.
DR EnsemblPlants; AT1G77760.1; AT1G77760.1; AT1G77760.
DR GeneID; 844112; -.
DR Gramene; AT1G77760.1; AT1G77760.1; AT1G77760.
DR KEGG; ath:AT1G77760; -.
DR Araport; AT1G77760; -.
DR TAIR; locus:2203221; AT1G77760.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_4_1_1; -.
DR InParanoid; P11832; -.
DR OMA; DTWSVCE; -.
DR OrthoDB; 166846at2759; -.
DR PhylomeDB; P11832; -.
DR BioCyc; MetaCyc:AT1G77760-MON; -.
DR PRO; PR:P11832; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P11832; baseline and differential.
DR Genevisible; P11832; AT.
DR GO; GO:0005829; C:cytosol; TAS:TAIR.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IBA:GO_Central.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IDA:CACAO.
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; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR012137; Nitr_rd_NADH.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
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; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
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 Disulfide bond; FAD; Flavoprotein; Heme; Herbicide resistance; Iron;
KW Metal-binding; Molybdenum; NAD; Nitrate assimilation; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..917
FT /note="Nitrate reductase [NADH] 1"
FT /id="PRO_0000166049"
FT DOMAIN 545..620
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 660..772
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P49050"
FT BINDING 580
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 603
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 712..715
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 729..733
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 734
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 741
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 746..748
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 799
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 436
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT MUTAGEN 198
FT /note="A->T: Loss of activity."
FT CONFLICT 17
FT /note="A -> R (in Ref. 1; CAA79494)"
FT /evidence="ECO:0000305"
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
