NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate 88069;
DOI=10.1007/BF00352105; PubMed=7614559 [NCBI, ExPASy, EBI, Israel, Japan]
Pieterse C.M.J., van 't Klooster J., van den Berg-Velthuis G.C.M., Govers F.;
"NiaA, the structural nitrate reductase gene of Phytophthora infestans: isolation, characterization and expression analysis in Aspergillus nidulans.";
Curr. Genet. 27:359-366(1995).

Comments

FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
CATALYTIC ACTIVITY: Nitrite + NADP⁺ + H₂O = nitrate + NADPH.
COFACTOR: Binds 1 FAD.
COFACTOR: Binds 1 heme group. The heme group is called cytochrome b-557.
COFACTOR: Binds 1 molybdenum ion.
SUBUNIT: Homodimer (By similarity).
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

U14405; AAA86681.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S57199; S57199.

3D structure databases

HSSP

P04166; 1EUE. [HSSP ENTRY / PDB]

ModBase

P39864.

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; FALSE_NEG.
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; NADP; Nitrate assimilation; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 902`	`902`	`Nitrate reductase [NADPH].`	`PRO_0000166047`
`DOMAIN`	`537 612`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`637 751`	`115`	`FAD-binding FR-type.`
`NP_BIND`	`872 879`	`8`	`NADP (By similarity).`
`METAL`	`182 182`		`Molybdenum-pterin (Potential).`
`METAL`	`234 234`		`Molybdenum-pterin (Potential).`
`METAL`	`572 572`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`595 595`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`419 419`		`Interchain (Potential).`

Sequence information

Length: 902 AA [This is the length of the unprocessed precursor]

Molecular weight: 101074 Da [This is the MW of the unprocessed precursor]

CRC64: 05B9F4E1A381BBE6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTRLRSAAST ITNRSTPALA LTASHAGSHP AVIVPIQPLL LTLERRPSCP HRVSYPEIEA 

        70         80         90        100        110        120 
YRGISSSLRS HNAIVRASDI MAQIDPRDVG TPDEWVPRHP ELIRLTGRHP FNSEPPLKYA 

       130        140        150        160        170        180 
STFITPMALH YVRNHGPVPR LEWDTHTFSI DGLVKKPRTF GMNELVTTFE QETVTFPVLL 

       190        200        210        220        230        240 
VCAGNRRKEQ NMIKKTIGFS WGAAGCSTAE WTGVPLHVLL TACGVDREKA QWVWFEGIED 

       250        260        270        280        290        300 
LPHDKYGTCI RASTELDPEC DVLVAWKANG ELLGPDHGFP VRLIVPGHIG GRMVKWLERI 

       310        320        330        340        350        360 
HVSDHESSNH HHIMDNRVLP SHVTAETATA EGWWSKSPYA IMELNVNAVV ILPNHDDLLA 

       370        380        390        400        410        420 
LGEDTTFNDI ETYTIKGYAY SGGGRRVIRV EVTLDDGASW QLARIIYHER PSKYGKMWCW 

       430        440        450        460        470        480 
VHYELAAPMS SLLCAREVCV RAWDSSMNLM PAFPTWNVMG MMNNPWYRVK IHHEQDTNSL 

       490        500        510        520        530        540 
RFEHPTQAGN QKGGWMTKER IMTNDVDSIK MLQVEPLDTS SAATPKPGLT ADELSELPLI 

       550        560        570        580        590        600 
FADEVAKHNS KKSCWFICRD LVYDATPFLD EHPGGATSIL LCGGTDCTDE FESIHSTKAW 

       610        620        630        640        650        660 
QMLKKYCIGR CSSTEDDTGT SDTSSDHEET DVALKGRTKV PIVLISREVV SHDARIFKFA 

       670        680        690        700        710        720 
LPAKDLRLGL PIGNHVFLYA KINGKTAVRA YTPISSENDE DRGFVSFLIK VYFAGDNPVH 

       730        740        750        760        770        780 
PEGGLFSQYL DGLHLGQQIQ IKGPLGHFTY YGDGNFSLET TNFHAYKFGF VAGGTGITPV 

       790        800        810        820        830        840 
YQVMRAILED AKDQTKVALI YCVRSQRDLL LRKELETLQK LRPGQCRIFY TLSDMELLDR 

       850        860        870        880        890        900 
NDPIVRGWAY GKSRLNFAMV KNIIGSDAED VCMCGPEGMI EYACKPALLK LNYDLKTQTT 


VF

P39864 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