Reviewed, UniProtKB/Swiss-Prot P11035 (NIA2_ARATH)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADH] 2
      Short name=NR2
    EC=1.7.1.1

Gene names

Name:	NIA2
Synonyms:	CHL3
Ordered Locus Names:	At1g37130
ORF Names:	F28L22.2

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(+) + H(2)O = 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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to herbicide Inferred from electronic annotation. Source: UniProtKB-KW
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 iron ion binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro 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] 2		PRO_0000166050
Regions
	Domain	542 – 617	76	Cytochrome b5 heme-binding
	Domain	660 – 772	113	FAD-binding FR-type
Sites
	Metal binding	191	1	Molybdenum-pterin Potential
	Metal binding	245	1	Molybdenum-pterin Potential
	Metal binding	577	1	Iron (heme axial ligand) By similarity
	Metal binding	600	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	433		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P11035-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: B8909A318C04C39A	FASTA	917	102,844
	10 20 30 40 50 60 MAASVDNRQY ARLEPGLNGV VRSYKPPVPG RSDSPKAHQN QTTNQTVFLK PAKVHDDDED 70 80 90 100 110 120 VSSEDENETH NSNAVYYKEM IRKSNAELEP SVLDPRDEYT ADSWIERNPS MVRLTGKHPF 130 140 150 160 170 180 NSEAPLNRLM HHGFITPVPL HYVRNHGHVP KAQWAEWTVE VTGFVKRPMK FTMDQLVSEF 190 200 210 220 230 240 AYREFAATLV CAGNRRKEQN MVKKSKGFNW GSAGVSTSVW RGVPLCDVLR RCGIFSRKGG 250 260 270 280 290 300 ALNVCFEGSE DLPGGAGTAG SKYGTSIKKE YAMDPSRDII LAYMQNGEYL TPDHGFPVRI 310 320 330 340 350 360 IIPGFIGGRM VKWLKRIIVT TKESDNFYHF KDNRVLPSLV DAELADEEGW WYKPEYIINE 370 380 390 400 410 420 LNINSVITTP CHEEILPINA FTTQRPYTLK GYAYSGGGKK VTRVEVTVDG GETWNVCALD 430 440 450 460 470 480 HQEKPNKYGK FWCWCFWSLE VEVLDLLSAK EIAVRAWDET LNTQPEKMIW NLMGMMNNCW 490 500 510 520 530 540 FRVKTNVCKP HKGEIGIVFE HPTLPGNESG GWMAKERHLE KSADAPPSLK KSVSTPFMNT 550 560 570 580 590 600 TAKMYSMSEV KKHNSADSCW IIVHGHIYDC TRFLMDHPGG SDSILINAGT DCTEEFEAIH 610 620 630 640 650 660 SDKAKKMLED YRIGELITTG YSSDSSSPNN SVHGSSAVFS LLAPIGEATP VRNLALVNPR 670 680 690 700 710 720 AKVPVQLVEK TSISHDVRKF RFALPVEDMV LGLPVGKHIF LCATINDKLC LRAYTPSSTV 730 740 750 760 770 780 DVVGYFELVV KIYFGGVHPR FPNGGLMSQY LDSLPIGSTL EIKGPLGHVE YLGKGSFTVH 790 800 810 820 830 840 GKPKFADKLA MLAGGTGITP VYQIIQAILK DPEDETEMYV IYANRTEEDI LLREELDGWA 850 860 870 880 890 900 EQYPDRLKVW YVVESAKEGW AYSTGFISEA IMREHIPDGL DGSALAMACG PPPMIQFAVQ 910 PNLEKMQYNI KEDFLIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains." Crawford N.M., Smith M., Bellissimo D.B., Davis R.W. Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988) [PubMed: 3393528] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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]	"Identification of the Arabidopsis CHL3 gene as the nitrate reductase structural gene NIA2." Wilkinson J.Q., Crawford N.M. Plant Cell 3:461-471(1991) [PubMed: 1840922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 350-422.
[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: 2905260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 522-917.
[6]	"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: HERBICIDE RESISTANCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03240 mRNA. Translation: AAA32830.1. AC007505 Genomic DNA. Translation: AAF19225.1. AF367272 mRNA. Translation: AAK56261.1. AF436835 mRNA. Translation: AAL32017.1. AY037183 mRNA. Translation: AAK59768.1. AY039914 mRNA. Translation: AAK64018.1. AY133530 mRNA. Translation: AAM91360.1. AY142568 mRNA. Translation: AAN13137.1. S45385 Genomic DNA. Translation: AAL32273.1. X13435 mRNA. Translation: CAA31787.1.
PIR	RDMUNH. A31821.
RefSeq	NP_174901.1.
UniGene	At.23731
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
ModBase	Search...
Proteomic databases
ProMEX	P11035.
Genome annotation databases
GeneID	840630.
GenomeReviews	Gene locus AT1G37130 in contig CT485782_GR.
KEGG	ath:AT1G37130.
Organism-specific databases
TAIR	At1g37130.
Gene expression databases
GermOnline	AT1G37130. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR001834. Cyt_B5_reductase. IPR001709. FPN_cyt_redctse. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. 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

NIA2_ARATH

Accession

Primary (citable) accession number: P11035
Secondary accession number(s): Q7Y260

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 25, 2008
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)