Reviewed, UniProtKB/Swiss-Prot P08509 (NIA2_TOBAC)

Names and origin

Protein names

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

Gene names

Name:

NIA2

Organism

Nicotiana tabacum (Common tobacco)

Taxonomic identifier

4097 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana

Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Enzyme regulation	Regulated by the nitrogen source and controlled by the circadian rhythm.
Subunit structure	Homodimer.
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	Nitrate assimilation
Ligand	FAD Flavoprotein Heme Iron Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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 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 – 904	904	Nitrate reductase [NADH] 2		PRO_0000166073
Regions
	Domain	531 – 606	76	Cytochrome b5 heme-binding
	Domain	647 – 759	113	FAD-binding FR-type
Sites
	Metal binding	183	1	Molybdenum-pterin Potential
	Metal binding	237	1	Molybdenum-pterin Potential
	Metal binding	566	1	Iron (heme axial ligand) By similarity
	Metal binding	589	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	422		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P08509-1 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: 75196875A3561D69	FASTA	904	101,958
	10 20 30 40 50 60 MAASVENRQF SHLEAGLSRS FKPRSDSPVR GCNFPSPNST NFQKKPNSTI YLDYSSSEDD 70 80 90 100 110 120 DDDDEKNEYL QMIKKGNSEL EPSVHDTRDE GTADNWIERN FSMIRLTGKH PFNSEPPLNR 130 140 150 160 170 180 LMHHGFITPV PLHYVRNHGP VPKGTWDDWT VEVTGLVKRP MKFTMDQLVN EFPCRELPVT 190 200 210 220 230 240 LVCAGNRRKE QNMVKQTIGF NWGAAAVSTT IWRGVPLRAL LKRCGVFSKN KGALNVCFEG 250 260 270 280 290 300 ADVLPGGGGS KYGTSIKKEF AMDPARDIIV AYMQNGEKLA PDHGFPVRMI IPGFIGGRMV 310 320 330 340 350 360 KWIKRIIVTT QESDSYYHFK DNRVLPPHVD AELANTEAWW YKPEYIINEL NINSVITTPC 370 380 390 400 410 420 HEEILPINAW TTQRPYTLRG YSYSGGGKKV TRVEVTLDGG ETWQVSTLDH PEKPTKYGKY 430 440 450 460 470 480 WCWCFWSLEV EVLDLLSAKE IAVRAWDETL NTQPEKLIWN VMGMMNNCWF RVKMNVCKPH 490 500 510 520 530 540 KGEIGIVFEH PTQPGNQSGG WMAKERHLEI SAEAPQTLKK SISTPFMNTA SKMYSMSEVR 550 560 570 580 590 600 KHSSADSAWI IVHGHIYDAT RFLKDHPGGT DSILINAGTD CTEEFDAIHS DKAKKLLEDF 610 620 630 640 650 660 RIGELITTGY TSDSPGNSVH GSSSFSSFLA PIKELVPAQR SVALIPREKI PCKLIDKQSI 670 680 690 700 710 720 SHDVRKFRFA LPSEDQVLGL PVGKHIFLCA VIDDKLCMRA YTPTSTIDEV GYFELVVKIY 730 740 750 760 770 780 FKGIHPKFPN GGQMSQYLDS MPLGSFLDVK GPLGHIEYQG KGNFLVHGKQ KFAKKLAMIA 790 800 810 820 830 840 GGTGITPVYQ VMQAILKDPE DDTEMYVVYA NRTEDDILLK EELDSWAEKI PERVKVWYVV 850 860 870 880 890 900 QDSIKEGWKY SIGFITEAIL REHIPEPSHT TLALACGPPP MIQFAVNPNL EKMGYDIKDS LLVF

References

[1]	"Complete nucleotide sequence of the two homeologous tobacco nitrate reductase genes." Vaucheret H., Kronenberger J., Rouze P., Caboche M. Plant Mol. Biol. 12:597-600(1989) Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Xanthi. Tissue: Leaf.
[2]	"Cloning of DNA fragments complementary to tobacco nitrate reductase mRNA and encoding epitopes common to the nitrate reductases from higher plants." Calza R., Huttner E., Vincentz M., Rouze P., Galangau F., Vaucheret H., Cherel I., Meyer C., Kronenberger J., Caboche M. Mol. Gen. Genet. 209:552-562(1987) [PubMed: 17193712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 171-724.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14059 Genomic DNA. Translation: CAA32217.1. X06134 mRNA. Translation: CAA29497.1.
PIR	RDNTNS. S04839.
3D structure databases
SMR	P08509. Positions 82-507, 532-605, 649-904.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.1. 298.
Family and domain databases
InterPro	IPR001199. Cyt_B5. 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. IPR017938. Riboflavin_synthase-like_b-brl. [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.
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_TOBAC

Accession

Primary (citable) accession number: P08509

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 1, 1989
Last modified:	January 19, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)