[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=16593773 [NCBI, ExPASy, EBI, Israel, Japan] Crawford N.M., Campbell W.H., Davis R.; "Nitrate reductase from squash: cDNA cloning and nitrate regulation."; Proc. Natl. Acad. Sci. U.S.A. 83:8073-8076(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Seedling; PubMed=1748631 [NCBI, ExPASy, EBI, Israel, Japan] Hyde G.E., Crawford N.M., Campbell W.H.; "The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases."; J. Biol. Chem. 266:23542-23547(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.
INDUCTION: By nitrate.
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

M33154; AAA33114.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41667; A41667.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P17569.

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`	`1 918`	`918`	`Nitrate reductase [NADH].`	`PRO_0000166055`
`DOMAIN`	`543 618`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`661 774`	`114`	`FAD-binding FR-type.`
`METAL`	`195 195`		`Molybdenum-pterin (Potential).`
`METAL`	`249 249`		`Molybdenum-pterin (Potential).`
`METAL`	`578 578`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`601 601`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`434 434`		`Interchain (Potential).`

Sequence information

Length: 918 AA [This is the length of the unprocessed precursor]

Molecular weight: 103384 Da [This is the MW of the unprocessed precursor]

CRC64: A2CAFDDADEA1B2D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVDNRQY GPLQPPLSGV VRSFKNGPNH RADSPVRGCN FPNSNVDYNN NRPLKSSVKI 

        70         80         90        100        110        120 
QEAAAEEMED SCSEDENENE FRDLIVKGNR ELEPSILDHR DEGTADNWIE RNASMVRLTG 

       130        140        150        160        170        180 
KHPFNSEPPL NRLMHHGFIT PVPLHYVRNH GVVPKAKWAD WTVEVCGLVK RPAKFTMDQL 

       190        200        210        220        230        240 
LNEFRFREFP ATLVCAGNRR KEQNMVKQSI GFNWGAAGVS TSVWRRVPLC DLLKRCGILS 

       250        260        270        280        290        300 
RKKGALNVCF EGAEDLPGGG GSKYGTSIKK ELAMDPARDI ILAYMQNGEQ LAPDHGFPVR 

       310        320        330        340        350        360 
MIIPGFIGGR MVKWLKRIIV TTKESENYYH FKDNRVLPSH VDADVANAEA WWYKPEHIIN 

       370        380        390        400        410        420 
ELNINSVITT PCHEEILPIN AWTTQRPYTL RGYSYSGGGK KVTRVEVTMD SGETWQVCTL 

       430        440        450        460        470        480 
DHPEKANKYG KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE THNTQPEKLI WNLMGMMNNC 

       490        500        510        520        530        540 
WFRVKTNMCK PHKGEIGIVF EHPTQPGNQS GGWMDRERHL EISTESNQTL KKSVSTPFMN 

       550        560        570        580        590        600 
TASNTYTLSE VKKHNSPQSA WIIVHGHVYD CTRFLKDHPG GSDSILINAG TDCTEEFDAI 

       610        620        630        640        650        660 
HSDKAKKMLE DYRIGELITT GYASDSSSNS PNNSTHGASN FSHLAPIREA PVSRRVALAP 

       670        680        690        700        710        720 
NEKIPCKLIS KTSISHDVRV FRFALPGGQD QALGLPVGKH IFICATVDGK LCMRAYTPTS 

       730        740        750        760        770        780 
SIDEMGFFEL VVKVYFKGVH PKFPNGGIMS QYLDSMEVGS TLDVKGPLGH IEYTGRGNFM 

       790        800        810        820        830        840 
VHGKPRFARR LAMLAGGTGI TPIYQVVQAI LKDPEDETEM YVVYANRTED DILLRDELDT 

       850        860        870        880        890        900 
WAKKNQRLKV WYVVQESIRE GWEYSVGFIT ENILREHIPA AAEDTLALAC GPPAMIQFAV 

       910 
QPNLEKMNYD TKNSLLVF

P17569 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