NUCLEOTIDE SEQUENCE.
STRAIN=cv. Xanthi;
TISSUE=Leaf;
Vaucheret H., Kronenberger J., Rouze P., Caboche M.;
"Complete nucleotide sequence of the two homeologous tobacco nitrate reductase genes.";
Plant Mol. Biol. 12:597-600(1989).

[2]

NUCLEOTIDE SEQUENCE OF 171-724.
DOI=10.1007/BF00331162; PubMed=17193712 [NCBI, ExPASy, EBI, Israel, Japan]
Calza R., Huttner E., Vincentz M., Rouze P., Galangau F., Vaucheret H., Cherel I., Meyer C., Kronenberger J., Caboche M.;
"Cloning of DNA fragments complementary to tobacco nitrate reductase mRNA and encoding epitopes common to the nitrate reductases from higher plants.";
Mol. Gen. Genet. 209:552-562(1987).

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.
COFACTOR: Binds 1 heme group per subunit.
COFACTOR: Binds 1 molybdenum-pterin group per subunit.
ENZYME REGULATION: Regulated by the nitrogen source and controlled by the circadian rhythm.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the nitrate reductase family.
SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14059; CAA32217.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X06134; CAA29497.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04839; RDNTNS.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P08509.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0009703;	Molecular function: nitrate reductase (NADH) activity (inferred from electronic annotation from EC).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.

Pfam

PF00173; Cyt-b5; 1.
PF00970; FAD_binding_6; 1.
PF03404; Mo-co_dimer; 1.
PF00175; NAD_binding_1; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000233; Nitr_rd_NADH; 1.

PRINTS

PR00406; CYTB5RDTASE.
PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
PR00371; FPNCR.

ProDom

PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS51384; FAD_FR; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P08509.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD; Nitrate assimilation; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 904`	`904`	`Nitrate reductase [NADH] 2.`	`PRO_0000166073`
`DOMAIN`	`531 606`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`647 759`	`113`	`FAD-binding FR-type.`
`METAL`	`183 183`		`Molybdenum-pterin (Potential).`
`METAL`	`237 237`		`Molybdenum-pterin (Potential).`
`METAL`	`566 566`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`589 589`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`422 422`		`Interchain (Potential).`

Sequence information

Length: 904 AA [This is the length of the unprocessed precursor]

Molecular weight: 101958 Da [This is the MW of the unprocessed precursor]

CRC64: 75196875A3561D69 [This is a checksum on the sequence]

        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

P08509 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools