NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Williams;
DOI=10.1007/BF00020980; PubMed=8534848 [NCBI, ExPASy, EBI, Israel, Japan]
Wu S., Lu Q., Kriz A.L., Harper J.E.;
"Identification of cDNA clones corresponding to two inducible nitrate reductase genes in soybean: analysis in wild-type and nr1 mutant.";
Plant Mol. Biol. 29:491-506(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 + NAD⁺ + H₂O = nitrate + NADH.
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

U13987; AAA96813.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S66308; S66308.

UniGene

Gma.8416

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

SMR

P39870; 636-890.

ModBase

P39870.

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`	`1 890`	`890`	`Inducible nitrate reductase [NADH] 2.`	`PRO_0000166070`
`DOMAIN`	`517 592`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`634 746`	`113`	`FAD-binding FR-type.`
`METAL`	`169 169`		`Molybdenum-pterin (Potential).`
`METAL`	`223 223`		`Molybdenum-pterin (Potential).`
`METAL`	`552 552`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`575 575`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`408 408`		`Interchain (Potential).`

Sequence information

Length: 890 AA [This is the length of the unprocessed precursor]

Molecular weight: 99945 Da [This is the MW of the unprocessed precursor]

CRC64: 3D1B373D9413F78C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVDQRPY PGLHNGVVRP LKPGPDIPRP KKLPQAPPPL SDSSSDEEED TTLNLKDLIR 

        70         80         90        100        110        120 
KGTTEVESSI FDPRDDGTSD HWIQRNSSLV RLTGKHPFNS EPPLPRLMHH GFITPVPLHY 

       130        140        150        160        170        180 
VRNHGPVPRA RWEDWTVEVT GLVTRPTCFT MEQLLHDFPS REFPATLVCA GNRRKEQNMV 

       190        200        210        220        230        240 
KQSIGFNWGA AAISTSVWRG VPLRTLLKSC GIYTRTKGAL HVCFEGAEDL PGGGGSKYGT 

       250        260        270        280        290        300 
SILREVALDP SRDIILAYMQ NGEPLSPDHG FPVRMIIPGF IGGRMVKWLK RIIVTTDQSQ 

       310        320        330        340        350        360 
NYYHYKDNRV LPSHVDAELA NAQAWWYKPD YIINELNINS VITTPCHEEI LPINSWTTQM 

       370        380        390        400        410        420 
PYFIRGYAYS GGGRKVTRVE VTLDGGETWQ VCTLDCPEKP NKYGKYWCWC LWSVEVEVLD 

       430        440        450        460        470        480 
LLGAREIAVR AWDEALNTQP EKLIWNVMGM MNNCWFRVKT NVCRPHKGEI GIVFEHPTQP 

       490        500        510        520        530        540 
GNQSGGWMAK EKHLEKSSES NPTLKKSVSS PFMNTTSKTY TMSEVRRHNN ADSAWIIVHG 

       550        560        570        580        590        600 
HVYDCTRFLK DHPGGTDSIL INAGTDCTEE FEAIHSDKAK QMLEDYRIGE LTTTCYNSDS 

       610        620        630        640        650        660 
SSSNPSVHGS SDTIPLTPIK EVITPMRSVA LNPREKIPCK LISKTSISHD VRLFRFALPS 

       670        680        690        700        710        720 
DDLLMGLPVG KHIFLCATVD EKLCMRAYTP TSSVHEVGYF DLVVKVYFKG VHPKFPTGGI 

       730        740        750        760        770        780 
MSQHLDSLPI GSVLDVKGPL GHIVYTGRGN FLVHGKPRFA TRLAMLAGGT GITPIYQVVR 

       790        800        810        820        830        840 
AILKDPEDCT EMHVVYANRT EDDILLKEEL DEWAKKYDRL KVWYVIQASI REGWEYSVGF 

       850        860        870        880        890 
ITESILTEHI PNASPDTLAL TCGPPPMIQF AVQPNLEKLG YDTQNNLLVF

P39870 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