[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Isolate 19; DOI=10.1007/BF00280180; PubMed=8041355 [NCBI, ExPASy, EBI, Israel, Japan] Williams R.S.B., Davis M.A., Howlett B.J.; "Nitrate reductase of the ascomycetous fungus, Leptosphaeria maculans: gene sequence and chromosomal location."; Mol. Gen. Genet. 244:1-8(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 886-893. STRAIN=Isolate 19; DOI=10.1016/0378-1119(95)00169-7; PubMed=7789806 [NCBI, ExPASy, EBI, Israel, Japan] Williams R.S.B., Davis M.A., Howlett B.J.; "The nitrate and nitrite reductase-encoding genes of Leptosphaeria maculans are closely linked and transcribed in the same direction."; Gene 158:153-154(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

U04445; AAA50579.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18793; AAA82740.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S46442; S46442.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P36842.

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

P36842.

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`	`1 893`	`893`	`Nitrate reductase [NADPH].`	`PRO_0000166045`
`DOMAIN`	`536 611`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`641 752`	`112`	`FAD-binding FR-type.`
`NP_BIND`	`863 872`	`10`	`NADP (By similarity).`
`METAL`	`170 170`		`Molybdenum-pterin (Potential).`
`METAL`	`221 221`		`Molybdenum-pterin (Potential).`
`METAL`	`571 571`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`594 594`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`418 418`		`Interchain (Potential).`

Sequence information

Length: 893 AA [This is the length of the unprocessed precursor]

Molecular weight: 99942 Da [This is the MW of the unprocessed precursor]

CRC64: 7686E3C9676DD2EF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVTTQQPAV VPLPSSPRLP IESHAGPRST QLPPSPPETV NGDDPKSITS TPAEPDFPLP 

        70         80         90        100        110        120 
PPANPKPQVL DIDKPTPDAH VPRDPRLIRL TGVHPFNTEP PLTDLYNEGF LTSPELFYVR 

       130        140        150        160        170        180 
NHGAVPEVQD EECLDWEFSI EGMVANPLKI TLRQLLEEYE NVTYPVTLVC AGNRRKEQNV 

       190        200        210        220        230        240 
VRKSKGFAWG AAGVSTALFT GVVMKDVIER AKPLRKAKYV CMEGADKLPN GYYGTSVKLN 

       250        260        270        280        290        300 
WVMDPNRGIM LAHKMNGENL SLDHGKPLRA VVPGQIGGRS VKWLKKLIVT AEPSDNWYHI 

       310        320        330        340        350        360 
YDNRVLPTMV DPDEAAKNPK WWMDERYAIY DLSPNSAIAF PAHEEKVVLA SAENSYNVRG 

       370        380        390        400        410        420 
YAYSGGGRRI TRCEVSLNKG KNWRLANIDY AEDKYRDFEG RELFGARLDM DWRETSFCWC 

       430        440        450        460        470        480 
FWNLDIATAE LRDANDILVR AMDEAMCIQP RDMYWSVLGM MNNPWYRITI HHEGDVLRFE 

       490        500        510        520        530        540 
HPTQPALIPG GWMERVKKAG GNLTNGQWGE QIEGQELENT AVEEVKEIKM TKDGVNRIVE 

       550        560        570        580        590        600 
LDELKWHESA EYPWFVVNDE VYDGTSFLEG HPGGAQSIIS AAGLDASDEF MAIHSETAKA 

       610        620        630        640        650        660 
MMPAYHIGTL SPTASKQLSL EEPTSKQASS SSLRPTFLDS RTWSKALLSS KTKVSWDTRI 

       670        680        690        700        710        720 
FRFKLDHASQ TLGLPTGQHL MIRLRDPVTR EAIIRSYTPI SQISEQGFCD VLIKIYADAP 

       730        740        750        760        770        780 
GREGGKMTKA LDSIPCGHWV DMKGPIGKFE YLGKGVCSIN GNERRVRSMK MICGGSGITP 

       790        800        810        820        830        840 
IYQVLRAILQ DSADSTHCTV LNGNRLEEDI LCREDLDRFA EENGERCTLV HTLTQAAEGW 

       850        860        870        880        890 
TGRRGRIGEE LLKEFCGTEE DGLVLVCGPE GLERSVKGLL SGMAWRDDDV IFF

P36842 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