NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(90)90178-T; PubMed=2205530 [NCBI, ExPASy, EBI, Israel, Japan]
Johnstone I.L., McCabe P.C., Greaves P., Gurr S.J., Cole G.E., Brow M.A.D., Unkles S.E., Clutterbuck A.J., Kinghorn J.R., Innis M.A.;
"Isolation and characterisation of the crnA-niiA-niaD gene cluster for nitrate assimilation in Aspergillus nidulans.";
Gene 90:181-192(1990).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC 4;
DOI=10.1038/nature04341; PubMed=16372000 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).

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

M58291; AAA33314.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000015; EAA65574.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0182; JH0182.

RefSeq

XP_658610.1; -.

3D structure databases

HSSP

P04166; 1ICC. [HSSP ENTRY / PDB]

ModBase

P22945.

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

P22945.

Genome annotation databases

GeneID

2876780; -.

KEGG

ani:AN1006.2; -.

Other

UniRef

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`	`1 873`	`873`	`Nitrate reductase [NADPH].`	`PRO_0000166042`
`DOMAIN`	`512 587`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`616 729`	`114`	`FAD-binding FR-type.`
`NP_BIND`	`843 852`	`10`	`NADP (By similarity).`
`METAL`	`150 150`		`Molybdenum-pterin (Potential).`
`METAL`	`201 201`		`Molybdenum-pterin (Potential).`
`METAL`	`547 547`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`570 570`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`397 397`		`Interchain (Potential).`

Sequence information

Length: 873 AA [This is the length of the unprocessed precursor]

Molecular weight: 97560 Da [This is the MW of the unprocessed precursor]

CRC64: BEE38281987A894C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTTVTQVRT GSIPKTLKTS QIRVEEQEIT ELDTADIPLP PPSKEPTEVL SLDKTTPDSH 

        70         80         90        100        110        120 
VPRDPRLIRL TGVHPFNVEP PLTALFQQGF LTPPELFYVR NHGPVPHVRD EDIPNWELRI 

       130        140        150        160        170        180 
EGLVEKPITL SFKQILQNYD QITAPITLVC AGNRRKEQNT VRKSKGFSWG SAALSTALFT 

       190        200        210        220        230        240 
GPMMADIIKS AKPLRRAKYV CMEGADNLPN GNYGTSIKLN WAMDPNRGIM LAHKMNGEDL 

       250        260        270        280        290        300 
RPDHGRPLRA VVPGQIGGRS VKWLKKLIIT DAPSDNWYHI YDNRVLPTMV TPDMSSQNPS 

       310        320        330        340        350        360 
WWRDERYAIY DLNVNSAAVY PQHKETLDLA AARPFYTAKG YAYAGGGRRI TRVEISLDKG 

       370        380        390        400        410        420 
KSWRLARIEY AEDKYRDFEG TLYGGRVDMA WREACFCWSF WSLDIPVSEL ASSDALLVRA 

       430        440        450        460        470        480 
MDEALSLQPK DMYWSVLGMM NNPWFRVKIT NENGRLLFEH PTDITGSSGW MEQIKKAGGD 

       490        500        510        520        530        540 
LTNGNWGERQ EGEEPVEAEP VVEVNMKKEG VTRIIDLEEF KKNSSDERPW FVVNGEVYDG 

       550        560        570        580        590        600 
TAFLEGHPGG AQSIISAAGT DASEEFLEIH SETAKKMMPD YHIGTLDKAS LEALRKGNAD 

       610        620        630        640        650        660 
TTDSSSDPRP TFLTPKAWTK ATLTKKTSVS SDTHIFTLSL EHPSQALGLP TGQHLMLKTP 

       670        680        690        700        710        720 
DPKSSSSGSI IRSYTPISPS DQLGMVDILI KIYAETPSIP GGKMTTALDT LPLGSVIECK 

       730        740        750        760        770        780 
GPTGRFEYLD RGRVLISGKE RFVKSFVMIC GGTGITPVFQ VLRAVMQDEQ DETKCVMLDG 

       790        800        810        820        830        840 
NRLEEDILLK NELDEFEALA GKKEKCKIVH TLTKGSESWT GRRGRIDEEL IRQHAGTPDR 

       850        860        870 
ETMVLVCGPE AMEKASKKIL LSLGWKEENL HYF

P22945 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