[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF00017743; PubMed=2103436 [NCBI, ExPASy, EBI, Israel, Japan] Prosser I.M., Lazarus C.M.; "Nucleotide sequence of a spinach nitrate reductase cDNA."; Plant Mol. Biol. 15:187-190(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Hoyo; DOI=10.1016/S0167-4838(97)00015-0; PubMed=9128133 [NCBI, ExPASy, EBI, Israel, Japan] Tamura N., Takahashi H., Takeba G., Satoi T., Nakagawa H.; "The nitrate reductase gene isolated from DNA of cultured spinach cells."; Biochim. Biophys. Acta 1338:151-155(1997).
[3]	NUCLEOTIDE SEQUENCE OF 287-926. STRAIN=cv. Hoyo; Shiraishi N., Kubo Y., Takeba K., Kiyota S., Sakano K., Nakagawa H.; "Sequence analysis of cloned cDNA and proteolytic fragments for nitrate reductase from Spinacia oleracea L."; Plant Cell Physiol. 32:1031-1038(1991).

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.
SUBUNIT: Homodimer.
INTERACTION:
P42643:GRF1 (xeno); NbExp=1; IntAct=EBI-876582, EBI-876602;
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

M32600; AAA34033.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D86226; BAA13047.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U08029; AAA18377.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S11868; RDSPNH.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P23312.

Protein-protein interaction databases

IntAct

P23312; -.

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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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

P23312.

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`	`1 926`	`926`	`Nitrate reductase [NADH].`	`PRO_0000166071`
`DOMAIN`	`551 626`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`670 782`	`113`	`FAD-binding FR-type.`
`METAL`	`204 204`		`Molybdenum-pterin (Potential).`
`METAL`	`258 258`		`Molybdenum-pterin (Potential).`
`METAL`	`586 586`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`609 609`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`443 443`		`Interchain (Potential).`
`CONFLICT`	`303 303`		`D -> A (in Ref. 2; BAA13047).`

Sequence information

Length: 926 AA [This is the length of the unprocessed precursor]

Molecular weight: 103971 Da [This is the MW of the unprocessed precursor]

CRC64: FF21DF01963F1AFC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVDRQYH PAPMSGVVRT PFSNHHRSDS PVRNGYTFSN PPSSNGVVKP GEKIKLVDNN 

        70         80         90        100        110        120 
SNSNNGSNNN NNRYDSDSEE DDDENEMNVW NEMIKKGNSE LEPSSVDSRD EGTADQWIER 

       130        140        150        160        170        180 
NPSMIRLTGK HPFNSEPPLT RLMHHGFLTP VPLHYVRNHG PVPNAKWEDW TVEVTGLVKR 

       190        200        210        220        230        240 
PIRFTMDQLV NDFQSREFPV TLVCAGNRRK EQNMTKQSIG FNWGSAAVST SVWRGVPLRD 

       250        260        270        280        290        300 
VLKRCGVMSS LKGALNVCFE GAEDLPGGGG SKYGTSVKRE FAMDPARDII LAYMQNGEKL 

       310        320        330        340        350        360 
SPDHGYPVRM IIPGFIGGRM VKWLKRIIVT TTESDNYYHY KDNRVLPSHV DAELANSEAW 

       370        380        390        400        410        420 
WYKQEYIINE LNVNSVITSP CHEEILPINA WTTQRPYTMR GYAYSGGGRK VTRVEVTMDG 

       430        440        450        460        470        480 
GDTWDICELD HQERGSKYGK FWCWCFWSLE VEVLDLLGAK EIGVRAWDES LNTQPEKLIW 

       490        500        510        520        530        540 
NVMGMMNNCW FRVKTNVCKP HKGEIGIVFE HPTQPGNKSG GWMARERHLE ISDSGPTLKR 

       550        560        570        580        590        600 
TASTPFMNTT SKMYSMSEVK KHNTADSAWI VVHGNVYNAT RFLKDHPGGS DSILINAGTD 

       610        620        630        640        650        660 
CTEEFDAIHS DKAKRLLEDF RIGELISTGY TSDSSSPGNS VHGGSVYSGL AGLAPITEAV 

       670        680        690        700        710        720 
PLRNVALNPR VKIPCKLIEK VSLSHDVRRF RFGLPSEDQV LGLPVGKHIF LCANVDDKLC 

       730        740        750        760        770        780 
MRAYTPSSTI DVVGYFDLVV KVYFKDVHPR FPNGGVMSQH LDSLSLGSIV DVKGPLGHIE 

       790        800        810        820        830        840 
YLGKGNFTVH GKPKFAKKLA MISGGTGITP IYQVMQAILK DPEDKTEMHV VYANRTEEDI 

       850        860        870        880        890        900 
LLREELDKWA DEFRDRVKVW YVVEKAEEGW KYDTGFISEK ILRDHVPAVG DDVLALTCGP 

       910        920 
PPMIQFAVQP NLDKMGFDIK EQLLIF

P23312 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