Nitrate reductase [NADH] 2 - Nicotiana tabacum (Common tobacco)

Preferred order of sections

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
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme 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 – 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)

Tools

P08509 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 75196875A3561D69
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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

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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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14059 Genomic DNA. Translation: CAA32217.1. X06134 mRNA. Translation: CAA29497.1.
PIR	RDNTNS. S04839.
3D structure databases
ProteinModelPortal	P08509.
SMR	P08509. Positions 649-904.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_dom. IPR022407. OxRdtase_Mopterin_BS. 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.
SUPFAM	SSF55856. Cyt_B5. 1 hit. SSF81296. Ig_E-set. 1 hit. SSF56524. Oxidored_molyb. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
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:	September 21, 2011
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents