NIA2_ARATH
ID NIA2_ARATH Reviewed; 917 AA.
AC P11035; Q7Y260;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Nitrate reductase [NADH] 2;
DE Short=NR2;
DE EC=1.7.1.1;
GN Name=NIA2; Synonyms=CHL3; OrderedLocusNames=At1g37130; ORFNames=F28L22.2;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=3393528; DOI=10.1073/pnas.85.14.5006;
RA Crawford N.M., Smith M., Bellissimo D.B., Davis R.W.;
RT "Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding
RT nitrate reductase, a metalloflavoprotein with three functional domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988).
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 [GENOMIC DNA] OF 350-422.
RX PubMed=1840922; DOI=10.2307/3869352;
RA Wilkinson J.Q., Crawford N.M.;
RT "Identification of the Arabidopsis CHL3 gene as the nitrate reductase
RT structural gene NIA2.";
RL Plant Cell 3:461-471(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 522-917.
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 [7]
RP HERBICIDE RESISTANCE.
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 [8]
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 [9]
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 -!- INTERACTION:
CC P11035; O80931: AS1; NbExp=4; IntAct=EBI-4451150, EBI-763232;
CC P11035; Q17TI5: BRX; NbExp=3; IntAct=EBI-4451150, EBI-4426649;
CC P11035; P11035: NIA2; NbExp=5; IntAct=EBI-4451150, EBI-4451150;
CC P11035; Q3E9D5: SAMDC4; NbExp=5; IntAct=EBI-4451150, EBI-25512418;
CC P11035; Q84MB2: TIFY8; NbExp=4; IntAct=EBI-4451150, EBI-4426557;
CC P11035; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-4451150, EBI-4424568;
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; J03240; AAA32830.1; -; mRNA.
DR EMBL; AC007505; AAF19225.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31891.1; -; Genomic_DNA.
DR EMBL; AF367272; AAK56261.1; -; mRNA.
DR EMBL; AF436835; AAL32017.1; -; mRNA.
DR EMBL; AY037183; AAK59768.1; -; mRNA.
DR EMBL; AY039914; AAK64018.1; -; mRNA.
DR EMBL; AY133530; AAM91360.1; -; mRNA.
DR EMBL; AY142568; AAN13137.1; -; mRNA.
DR EMBL; AH004061; AAL32273.1; -; Genomic_DNA.
DR EMBL; X13435; CAA31787.1; -; mRNA.
DR PIR; A31821; RDMUNH.
DR RefSeq; NP_174901.1; NM_103364.3.
DR AlphaFoldDB; P11035; -.
DR SMR; P11035; -.
DR BioGRID; 25859; 20.
DR IntAct; P11035; 6.
DR STRING; 3702.AT1G37130.1; -.
DR iPTMnet; P11035; -.
DR MetOSite; P11035; -.
DR PaxDb; P11035; -.
DR PRIDE; P11035; -.
DR ProteomicsDB; 250558; -.
DR EnsemblPlants; AT1G37130.1; AT1G37130.1; AT1G37130.
DR GeneID; 840630; -.
DR Gramene; AT1G37130.1; AT1G37130.1; AT1G37130.
DR KEGG; ath:AT1G37130; -.
DR Araport; AT1G37130; -.
DR TAIR; locus:2029677; AT1G37130.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_4_1_1; -.
DR InParanoid; P11035; -.
DR OMA; THNSNAV; -.
DR OrthoDB; 166846at2759; -.
DR PhylomeDB; P11035; -.
DR BioCyc; MetaCyc:AT1G37130-MON; -.
DR BRENDA; 1.7.1.1; 399.
DR PRO; PR:P11035; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P11035; baseline and differential.
DR Genevisible; P11035; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IDA:TAIR.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IDA: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 GO; GO:0009610; P:response to symbiotic fungus; IEP: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] 2"
FT /id="PRO_0000166050"
FT DOMAIN 542..617
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 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
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 577
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 600
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 433
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 917 AA; 102844 MW; B8909A318C04C39A CRC64;
MAASVDNRQY ARLEPGLNGV VRSYKPPVPG RSDSPKAHQN QTTNQTVFLK PAKVHDDDED
VSSEDENETH NSNAVYYKEM IRKSNAELEP SVLDPRDEYT ADSWIERNPS MVRLTGKHPF
NSEAPLNRLM HHGFITPVPL HYVRNHGHVP KAQWAEWTVE VTGFVKRPMK FTMDQLVSEF
AYREFAATLV CAGNRRKEQN MVKKSKGFNW GSAGVSTSVW RGVPLCDVLR RCGIFSRKGG
ALNVCFEGSE DLPGGAGTAG SKYGTSIKKE YAMDPSRDII LAYMQNGEYL TPDHGFPVRI
IIPGFIGGRM VKWLKRIIVT TKESDNFYHF KDNRVLPSLV DAELADEEGW WYKPEYIINE
LNINSVITTP CHEEILPINA FTTQRPYTLK GYAYSGGGKK VTRVEVTVDG GETWNVCALD
HQEKPNKYGK FWCWCFWSLE VEVLDLLSAK EIAVRAWDET LNTQPEKMIW NLMGMMNNCW
FRVKTNVCKP HKGEIGIVFE HPTLPGNESG GWMAKERHLE KSADAPPSLK KSVSTPFMNT
TAKMYSMSEV KKHNSADSCW IIVHGHIYDC TRFLMDHPGG SDSILINAGT DCTEEFEAIH
SDKAKKMLED YRIGELITTG YSSDSSSPNN SVHGSSAVFS LLAPIGEATP VRNLALVNPR
AKVPVQLVEK TSISHDVRKF RFALPVEDMV LGLPVGKHIF LCATINDKLC LRAYTPSSTV
DVVGYFELVV KIYFGGVHPR FPNGGLMSQY LDSLPIGSTL EIKGPLGHVE YLGKGSFTVH
GKPKFADKLA MLAGGTGITP VYQIIQAILK DPEDETEMYV IYANRTEEDI LLREELDGWA
EQYPDRLKVW YVVESAKEGW AYSTGFISEA IMREHIPDGL DGSALAMACG PPPMIQFAVQ
PNLEKMQYNI KEDFLIF
