NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=cv. Witloof;
TISSUE=Leaf, and Root;
DOI=10.1007/BF00196644; PubMed=8987617 [NCBI, ExPASy, EBI, Israel, Japan]
Palms B., Goupil P., de Almeida Engler J., Van der Straeten D., Van Montagu M., Rambour S.;
"Evidence for the nitrate-dependent spatial regulation of the nitrate reductase gene in chicory roots.";
Planta 200:20-27(1996).

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 (By similarity).
TISSUE SPECIFICITY: In cortical cells of roots grown at low nitrate concentrations, in vascular tissues of roots at high nitrate concentrations and in root apex under both conditions.
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

X84103; CAA58909.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X84102; CAA58908.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S52301; S52301.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

SMR

P43101; 665-920.

ModBase

P43101.

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).

Other

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`	`1 920`	`920`	`Nitrate reductase [NADH].`	`PRO_0000166054`
`DOMAIN`	`534 609`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`663 775`	`113`	`FAD-binding FR-type.`
`METAL`	`185 185`		`Molybdenum-pterin (Potential).`
`METAL`	`239 239`		`Molybdenum-pterin (Potential).`
`METAL`	`569 569`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`592 592`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`424 424`		`Interchain (Potential).`

Sequence information

Length: 920 AA [This is the length of the unprocessed precursor]

Molecular weight: 103520 Da [This is the MW of the unprocessed precursor]

CRC64: FE1E332CCC9A4D58 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVENRQF RHEPGLSAAG VVRSFSPNHR RSDSPIRNCN YPAAAREFMT PKKLPPETYD 

        70         80         90        100        110        120 
TSDDEEDEAD YRDAIKKSNS ELESSVFDPR DQGTADQWIE RNPSMVRLTG KHPFNSEPPL 

       130        140        150        160        170        180 
NKLMQHGFIT PDPLHYVRNH GPVPNATWED WTVEICGLVK RPARFSMTQL VNEFPSREFP 

       190        200        210        220        230        240 
VTLVCAGNRR KEQNLTKQTI GFNWGAAGIS TSVWKGVPLV HILKRCGIYS RKKGALNVCF 

       250        260        270        280        290        300 
EGAEDLPGGG GSKYGTSIKI EMAMDPARDI ILAYMQNGEK LSPDHGFPVR MIIPGFIGGR 

       310        320        330        340        350        360 
MVKWLKRIIV TTPESESYYH FKDNRVLPSH VDAELANSEG WWYKPEYIIN ELNINSVITT 

       370        380        390        400        410        420 
PCHEEILPIN SWTTQRPYTL RGYAYSGGGK KVTRVEVTMD GGETWNVCTL DHKEKPTRYA 

       430        440        450        460        470        480 
KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE TLNTQPDKLI WNLMGMMNNC WFRVKTNMCK 

       490        500        510        520        530        540 
PHKGEIGIVF EHPTQPGNQS GGWMAREKHL EISSELAHPT LKKSVSSPFM NTTSLTFTMS 

       550        560        570        580        590        600 
EVKKHNSADS AWIVVHGHIY DCTSFLKDHP GGSDSILLNA GTDCTEEFDA IHSDKAKKLL 

       610        620        630        640        650        660 
EEYRVGELIT MGYSSDSAAS SPNNSVHGAT NYLTLHLSLA TIKEIAPTRS VALIPKEIAP 

       670        680        690        700        710        720 
TRREKIPCKL ISKTSVSHDV RLFRFALPSP DQVLGLPVGK HVFVCATIDD KLCMRAYTPT 

       730        740        750        760        770        780 
STIDEVGYFE LLVKIYFKGV EPKFPNGGLM SQHLESMELG SSIEIKGPLG HIEYMGRGTF 

       790        800        810        820        830        840 
SVHGKQKFAR KLAMFAGGTG ITPDLSSDAS YLKDPEDDTE MYVVYANRTE DDILLREELD 

       850        860        870        880        890        900 
AWADKYSDRV KVWYVVAKSI REGWKYSEGF ITEDIMREHV PEVSEDTLAL ACGPPPMIQF 

       910        920 
AINPNLEKMG YDIKNSLLVF

P43101 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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