NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(92)90682-F; PubMed=1541396 [NCBI, ExPASy, EBI, Israel, Japan]
Unkles S.E., Campbell E.I., Punt P.J., Hawker K.L., Contreras R., Hawkins A.R., van den Hondel C.A.M.J.J., Kinghorn J.R.;
"The Aspergillus niger niaD gene encoding nitrate reductase: upstream nucleotide and amino acid sequence comparisons.";
Gene 111:149-155(1992).

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

M77022; -; NOT_ANNOTATED_CDS; Genomic_DNA.

[EMBL / GenBank / DDBJ]

PIR

JQ1525; JQ1525.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P36858.

Ontologies

GO:0050464;	Molecular function: nitrate reductase (NADPH) activity (inferred from electronic annotation from EC).
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).

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`	`1 867`	`867`	`Nitrate reductase [NADPH].`	`PRO_0000166040`
`DOMAIN`	`514 589`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`615 726`	`112`	`FAD-binding FR-type.`
`NP_BIND`	`837 846`	`10`	`NADP (By similarity).`
`METAL`	`152 152`		`Molybdenum-pterin (Potential).`
`METAL`	`203 203`		`Molybdenum-pterin (Potential).`
`METAL`	`549 549`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`572 572`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`399 399`		`Interchain (Potential).`

Sequence information

Length: 867 AA [This is the length of the unprocessed precursor]

Molecular weight: 97189 Da [This is the MW of the unprocessed precursor]

CRC64: BE40335DCBE12E42 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATVTEVLTE PFTAQGVTLK SGPIKVHQEE LPAVELSDIP LPPPSKEPTE VLSIDKPTPD 

        70         80         90        100        110        120 
YHVPRDPRLI RLTGVHPFNV EPPLTALYDE GFLTSPELFY VRNHGPVPLV KDEDIPNWEI 

       130        140        150        160        170        180 
SIEGLVEKPL VLNFRDILQQ YDQITAPITL VCAGNRRKEQ NVVRKTKGFS WGSAGLSTAL 

       190        200        210        220        230        240 
WTGPMMADIL RSAKPLRKAK YVCMEGADKL PNGYYGTSIK LNWAMDPNRG IMLAHKMNGE 

       250        260        270        280        290        300 
DLRPDHGRPL RAVVPGQIGG RSVKWLKKLI LTDAPSDNWY HIYDNRVLPT MVSPEMSSSD 

       310        320        330        340        350        360 
PNWWRDDRYA IYDLNVNSSV VYPEHKEVLD LASAGPSYNV KGYAYAGGGR RITRVEISLD 

       370        380        390        400        410        420 
KGKSWRLANI SYAEDKYRDF EGDLFGGRVH MSWRETCFCW CFWSLDIAIP ELENTDAILV 

       430        440        450        460        470        480 
RAMDEALALQ PRDMYWSVLG MMNNPWFRVT ITKENGTLRF EHPTDPTGPG GWMERVKKAG 

       490        500        510        520        530        540 
GDLVNGYWGE RQAGEEPTEP EPEKEINMKK EGVNRIIDLQ EFKKNSSDEK PWFIVNGEVY 

       550        560        570        580        590        600 
DGTAFLEGHP GGAQSIISSA GIDVSEEFLA IHTQTAKAMM PDYHIGTMDK ASLEALKNDN 

       610        620        630        640        650        660 
APQSDEPRAT FLQSKSWTKA TLVKRTDVSW DTRIFTFQLQ HDKQTLGLPI GQHLMIKVAD 

       670        680        690        700        710        720 
PTSKEAIIRS YTPISDTNQE GTMDLLVKIY FDTPTVKGGK MTMALEKLAL GSEIDCKGPT 

       730        740        750        760        770        780 
GRFEYLGNGK ILVSGKERHV SSFKMICGGT GITPIFQVLR AVMQDKQDPT SCVVLDGNRQ 

       790        800        810        820        830        840 
EEDILCRADL DAYEALDSKK CKVVHTLTKA PDSWTGRRGR ISEDLLKEHA IPDGKSMVLI 

       850        860 
CGPEAMEKSA RKILLEQGWA ESDLHFF

P36858 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