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Protein

Nitrate reductase [NADH] 1

Gene

NIA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activityi

Nitrite + NAD+ + H2O = nitrate + NADH.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • hemeBy similarityNote: Binds 1 heme group per subunit.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi197 – 1971MolybdenumBy similarity
Metal bindingi580 – 5801Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi603 – 6031Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • nitrate assimilation Source: TAIR
  • nitric oxide biosynthetic process Source: TAIR
  • response to herbicide Source: UniProtKB-KW
  • response to light stimulus Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Herbicide resistance, Nitrate assimilation

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyciMetaCyc:AT1G77760-MONOMER.
ReactomeiR-ATH-114608. Platelet degranulation.
R-ATH-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-ATH-196836. Vitamin C (ascorbate) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADH] 1 (EC:1.7.1.1)
Short name:
NR1
Gene namesi
Name:NIA1
Ordered Locus Names:At1g77760
ORF Names:T32E8.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G77760.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981A → T: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 917917Nitrate reductase [NADH] 1PRO_0000166049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi436 – 436InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP11832.
PRIDEiP11832.

PTM databases

iPTMnetiP11832.

Expressioni

Tissue specificityi

Root, leaf, and shoot.

Gene expression databases

GenevisibleiP11832. AT.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi29331. 8 interactions.
IntActiP11832. 4 interactions.
STRINGi3702.AT1G77760.1.

Structurei

3D structure databases

ProteinModelPortaliP11832.
SMRiP11832. Positions 118-490, 549-604, 662-917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini545 – 62076Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini660 – 772113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the nitrate reductase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410JWE3. Eukaryota.
KOG0534. Eukaryota.
KOG0535. Eukaryota.
KOG0537. Eukaryota.
COG0543. LUCA.
COG2041. LUCA.
COG5274. LUCA.
HOGENOMiHOG000252609.
InParanoidiP11832.
KOiK10534.
OMAiQESAWIV.
PhylomeDBiP11832.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR012137. Nitr_rd_NADH.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PIRSFiPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSVDNRHY PTMNGVAHAF KPPLVPSPRS FDRHRHQNQT LDVILTETKI
60 70 80 90 100
VKETEVITTV VDSYDDSSSD DEDESHNRNV PYYKELVKKS NSDLEPSILD
110 120 130 140 150
PRDESTADSW IQRNSSMLRL TGKHPFNAEA PLPRLMHHGF ITPVPLHYVR
160 170 180 190 200
NHGAVPKANW SDWSIEITGL VKRPAKFTME ELISEFPSRE FPVTLVCAGN
210 220 230 240 250
RRKEQNMVKQ TIGFNWGSAG VSTSLWKGIP LSEILRRCGI YSRRGGALNV
260 270 280 290 300
CFEGAEDLPG GGGSKYGTSI KKEMAMDPAR DIILAYMQNG ELLTPDHGFP
310 320 330 340 350
VRVIVPGFIG GRMVKWLKRI IVTPQESDSY YHYKDNRVLP SLVDAELANS
360 370 380 390 400
EAWWYKPEYI INELNINSVI TTPGHAEILP INAFTTQKPY TLKGYAYSGG
410 420 430 440 450
GKKVTRVEVT LDGGDTWSVC ELDHQEKPNK YGKFWCWCFW SLDVEVLDLL
460 470 480 490 500
SAKDVAVRAW DESFNTQPDK LIWNLMGMMN NCWFRIRTNV CKPHRGEIGI
510 520 530 540 550
VFEHPTRPGN QSGGWMAKER QLEISSESNN TLKKSVSSPF MNTASKMYSI
560 570 580 590 600
SEVRKHNTAD SAWIIVHGHI YDCTRFLKDH PGGTDSILIN AGTDCTEEFE
610 620 630 640 650
AIHSDKAKKL LEDYRIGELI TTGYDSSPNV SVHGASNFGP LLAPIKELTP
660 670 680 690 700
QKNIALVNPR EKIPVRLIEK TSISHDVRKF RFALPSEDQQ LGLPVGKHVF
710 720 730 740 750
VCANINDKLC LRAYTPTSAI DAVGHIDLVV KVYFKDVHPR FPNGGLMSQH
760 770 780 790 800
LDSLPIGSMI DIKGPLGHIE YKGKGNFLVS GKPKFAKKLA MLAGGTGITP
810 820 830 840 850
IYQIIQSILS DPEDETEMYV VYANRTEDDI LVREELEGWA SKHKERLKIW
860 870 880 890 900
YVVEIAKEGW SYSTGFITEA VLREHIPEGL EGESLALACG PPPMIQFALQ
910
PNLEKMGYNV KEDLLIF
Length:917
Mass (Da):103,041
Last modified:June 6, 2002 - v3
Checksum:i6FD3ED46B9F63825
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171A → R in CAA79494 (PubMed:8510658).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19050 Genomic DNA. Translation: CAA79494.1.
AC012193 Genomic DNA. Translation: AAG51627.1.
CP002684 Genomic DNA. Translation: AEE36018.1.
AY090950 mRNA. Translation: AAM13997.1.
AF424624 mRNA. Translation: AAL11617.1.
BT000989 mRNA. Translation: AAN41389.1.
X13434 mRNA. Translation: CAA31786.1.
X13436 Genomic DNA. Translation: CAA31788.1.
PIRiE96807.
S35228.
RefSeqiNP_177899.1. NM_106425.2.
UniGeneiAt.17771.

Genome annotation databases

EnsemblPlantsiAT1G77760.1; AT1G77760.1; AT1G77760.
GeneIDi844112.
GrameneiAT1G77760.1; AT1G77760.1; AT1G77760.
KEGGiath:AT1G77760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19050 Genomic DNA. Translation: CAA79494.1.
AC012193 Genomic DNA. Translation: AAG51627.1.
CP002684 Genomic DNA. Translation: AEE36018.1.
AY090950 mRNA. Translation: AAM13997.1.
AF424624 mRNA. Translation: AAL11617.1.
BT000989 mRNA. Translation: AAN41389.1.
X13434 mRNA. Translation: CAA31786.1.
X13436 Genomic DNA. Translation: CAA31788.1.
PIRiE96807.
S35228.
RefSeqiNP_177899.1. NM_106425.2.
UniGeneiAt.17771.

3D structure databases

ProteinModelPortaliP11832.
SMRiP11832. Positions 118-490, 549-604, 662-917.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29331. 8 interactions.
IntActiP11832. 4 interactions.
STRINGi3702.AT1G77760.1.

PTM databases

iPTMnetiP11832.

Proteomic databases

PaxDbiP11832.
PRIDEiP11832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G77760.1; AT1G77760.1; AT1G77760.
GeneIDi844112.
GrameneiAT1G77760.1; AT1G77760.1; AT1G77760.
KEGGiath:AT1G77760.

Organism-specific databases

TAIRiAT1G77760.

Phylogenomic databases

eggNOGiENOG410JWE3. Eukaryota.
KOG0534. Eukaryota.
KOG0535. Eukaryota.
KOG0537. Eukaryota.
COG0543. LUCA.
COG2041. LUCA.
COG5274. LUCA.
HOGENOMiHOG000252609.
InParanoidiP11832.
KOiK10534.
OMAiQESAWIV.
PhylomeDBiP11832.

Enzyme and pathway databases

BioCyciMetaCyc:AT1G77760-MONOMER.
ReactomeiR-ATH-114608. Platelet degranulation.
R-ATH-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-ATH-196836. Vitamin C (ascorbate) metabolism.

Miscellaneous databases

PROiP11832.

Gene expression databases

GenevisibleiP11832. AT.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR012137. Nitr_rd_NADH.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PIRSFiPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a chlorate-resistant mutant of Arabidopsis thaliana with mutations in both nitrate reductase structural genes NIA1 and NIA2."
    Wilkinson J.Q., Crawford N.M.
    Mol. Gen. Genet. 239:289-297(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT THR-198, HERBICIDE RESISTANCE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "A new locus (NIA 1) in Arabidopsis thaliana encoding nitrate reductase."
    Cheng C., Dewdney J., Nam H., den Boer B.G.W., Goodman H.M.
    EMBO J. 7:3309-3314(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 342-360 AND 525-917.
  6. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNIA1_ARATH
AccessioniPrimary (citable) accession number: P11832
Secondary accession number(s): Q9CA18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: June 6, 2002
Last modified: July 6, 2016
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

When mutated confers resistance to the herbicide chlorate.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.