Reviewed, UniProtKB/Swiss-Prot P11832 (NIA1_ARATH)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADH] 1
      Short name=NR1
    EC=1.7.1.1

Gene names

Name:	NIA1
Ordered Locus Names:	At1g77760
ORF Names:	T32E8.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	917 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activity	Nitrite + NAD+ + H2O = nitrate + NADH.
Cofactor	Binds 1 FAD per subunit. Binds 1 heme group per subunit. Binds 1 molybdenum-pterin group per subunit.
Subunit structure	Homodimer.
Tissue specificity	Root, leaf, and shoot.
Miscellaneous	When mutated confers resistance to the herbicide chlorate.
Sequence similarities	Belongs to the nitrate reductase family. Contains 1 cytochrome b5 heme-binding domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Herbicide resistance Nitrate assimilation
Ligand	FAD Flavoprotein Heme Iron Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nitrate assimilation Ref.1 Inferred from mutant phenotype. Source: TAIR nitric oxide biosynthetic process Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to herbicide Inferred from electronic annotation. Source: UniProtKB-KW response to light stimulus Inferred from mutant phenotype. Source: TAIR
Cellular component	cytosol Traceable author statement. Source: TAIR
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase (NADH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 917	917	Nitrate reductase [NADH] 1		PRO_0000166049
Regions
	Domain	545 – 620	76	Cytochrome b5 heme-binding
	Domain	660 – 772	113	FAD-binding FR-type
Sites
	Metal binding	197	1	Molybdenum-pterin Potential
	Metal binding	251	1	Molybdenum-pterin Potential
	Metal binding	580	1	Iron (heme axial ligand) By similarity
	Metal binding	603	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	436		Interchain Potential
Experimental info
	Mutagenesis	198	1	A → T: Loss of activity.
	Sequence conflict	17	1	A → R in CAA79494. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11832-1 [UniParc]. Last modified June 6, 2002. Version 3. Checksum: 6FD3ED46B9F63825	FASTA	917	103,041
	10 20 30 40 50 60 MATSVDNRHY PTMNGVAHAF KPPLVPSPRS FDRHRHQNQT LDVILTETKI VKETEVITTV 70 80 90 100 110 120 VDSYDDSSSD DEDESHNRNV PYYKELVKKS NSDLEPSILD PRDESTADSW IQRNSSMLRL 130 140 150 160 170 180 TGKHPFNAEA PLPRLMHHGF ITPVPLHYVR NHGAVPKANW SDWSIEITGL VKRPAKFTME 190 200 210 220 230 240 ELISEFPSRE FPVTLVCAGN RRKEQNMVKQ TIGFNWGSAG VSTSLWKGIP LSEILRRCGI 250 260 270 280 290 300 YSRRGGALNV CFEGAEDLPG GGGSKYGTSI KKEMAMDPAR DIILAYMQNG ELLTPDHGFP 310 320 330 340 350 360 VRVIVPGFIG GRMVKWLKRI IVTPQESDSY YHYKDNRVLP SLVDAELANS EAWWYKPEYI 370 380 390 400 410 420 INELNINSVI TTPGHAEILP INAFTTQKPY TLKGYAYSGG GKKVTRVEVT LDGGDTWSVC 430 440 450 460 470 480 ELDHQEKPNK YGKFWCWCFW SLDVEVLDLL SAKDVAVRAW DESFNTQPDK LIWNLMGMMN 490 500 510 520 530 540 NCWFRIRTNV CKPHRGEIGI VFEHPTRPGN QSGGWMAKER QLEISSESNN TLKKSVSSPF 550 560 570 580 590 600 MNTASKMYSI SEVRKHNTAD SAWIIVHGHI YDCTRFLKDH PGGTDSILIN AGTDCTEEFE 610 620 630 640 650 660 AIHSDKAKKL LEDYRIGELI TTGYDSSPNV SVHGASNFGP LLAPIKELTP QKNIALVNPR 670 680 690 700 710 720 EKIPVRLIEK TSISHDVRKF RFALPSEDQQ LGLPVGKHVF VCANINDKLC LRAYTPTSAI 730 740 750 760 770 780 DAVGHIDLVV KVYFKDVHPR FPNGGLMSQH LDSLPIGSMI DIKGPLGHIE YKGKGNFLVS 790 800 810 820 830 840 GKPKFAKKLA MLAGGTGITP IYQIIQSILS DPEDETEMYV VYANRTEDDI LVREELEGWA 850 860 870 880 890 900 SKHKERLKIW YVVEIAKEGW SYSTGFITEA VLREHIPEGL EGESLALACG PPPMIQFALQ 910 PNLEKMGYNV KEDLLIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8510658] [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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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: 2905260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 342-360 AND 525-917.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z19050 Genomic DNA. Translation: CAA79494.1. AC012193 Genomic DNA. Translation: AAG51627.1. 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.
IPI	IPI00518959.
PIR	E96807. S35228.
RefSeq	NP_177899.1.
UniGene	At.17771
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
ModBase	Search...
Proteomic databases
PRIDE	P11832.
Genome annotation databases
GeneID	844112.
GenomeReviews	Gene locus AT1G77760 in contig CT485782_GR.
KEGG	ath:AT1G77760.
NMPDR	fig|3702.1.peg.7318.
Organism-specific databases
TAIR	At1g77760.
Phylogenomic databases
OMA	P11832. SETAKAM.
Enzyme and pathway databases
BRENDA	1.7.1.1. 302.
Gene expression databases
ArrayExpress	P11832.
GermOnline	AT1G77760. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR001834. NADH-Cyt_B5_reductase. IPR012137. Nitr_rd_NADH. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit. G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit. G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.
Pfam	PF00173. 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]
PIRSF	PIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTS	PR00406. CYTB5RDTASE. PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN. PR00371. FPNCR.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. PS51384. FAD_FR. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIA1_ARATH

Accession

Primary (citable) accession number: P11832
Secondary accession number(s): Q9CA18

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	June 6, 2002
Last modified:	June 16, 2009
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)