[1]	NUCLEOTIDE SEQUENCE. STRAIN=cv. Saxa; Jensen P.E., Hoff T., Stummann B.M., Henningsen K.W.; Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.

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

U01029; AAA95940.1; -; Unassigned_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T11805; T11805.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P39866.

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`	`Nitrate reductase [NADH] 2.`	`PRO_0000166068`
`DOMAIN`	`513 588`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`634 746`	`113`	`FAD-binding FR-type.`
`METAL`	`165 165`		`Molybdenum-pterin (Potential).`
`METAL`	`219 219`		`Molybdenum-pterin (Potential).`
`METAL`	`548 548`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`571 571`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`404 404`		`Interchain (Potential).`

Sequence information

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

Molecular weight: 99995 Da [This is the MW of the unprocessed precursor]

CRC64: FC03B96F0139DE1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVGNRQF ATHMNGVVRS CGQDLKPSLP LDFDLDSSSS DDDENDDASY LKELVRKANA 

        70         80         90        100        110        120 
ETEASVMDPR DEGTADQWVA RNASMVRLTG KHPFNAESPL QRLMHHGFIT PVPLHYVRNH 

       130        140        150        160        170        180 
GPVPKANWED WTVEITGLVK RPTRFTMDRL VREFPHREFP ATLVCAGNRR KEQNMVKKTI 

       190        200        210        220        230        240 
GFNWGSAGTS TSVWRGVPVR HVLRRCGILT RGKGALHVSF EGAENLPGGG GSKYGTSISR 

       250        260        270        280        290        300 
EMAMDPSRDI ILAYMQNGEP LAPDHGFPIR MIIPGFIGGR MVKWLKRIVV TEQECESHYH 

       310        320        330        340        350        360 
YKDNRVLPSH VDPELANEEG WWFKPEYIIN ELNINSVITT PCHDEILPIN SWTTQRPYVV 

       370        380        390        400        410        420 
RGYAYSGGGR KVTRVEVTLD GGETWHVCTL DHPEKPNKYG KYWCWCFWSL EVEVLDLLGT 

       430        440        450        460        470        480 
KEIAVRAWDE GLNTQPENLI WNLMGMMNNC WFRVKTNVCK PHKGEIGIVF EHPTQPGNQP 

       490        500        510        520        530        540 
GGWMAKEKHL EQSQEAKPSL KKSVSTPFMN TASKMFSVSE VKKHSSPDSA WIIVHGHVYD 

       550        560        570        580        590        600 
CTRFLKDHPG GTDSILINAG TDCTEEFDAI HSDKAKKMLE DYRIGELITT GYTSADSSPN 

       610        620        630        640        650        660 
NSVHGNSEFI HLAPINEITT IPPLPPRSVA LNPRQKIPCK LVSKTSISHD VRLFRFEMPS 

       670        680        690        700        710        720 
KNQLLGLPVG KHIFLCATID GKLCMRAYTP TSSVEEVGFF DLLIKVYFKD VHPKFPNGGL 

       730        740        750        760        770        780 
MSQYLESLSI GSMLDVKGPL GHIEYTGRGN FTVNGKSRFA KRLAMLAGGT GITPIYQVAQ 

       790        800        810        820        830        840 
AILKDPEDLT EMHVVYANRT EDDILLREEL DTWAKEHCER FKVWYVVETA KEGWGYGVGF 

       850        860        870        880        890 
ITEAIMREHL PEASSDSLAM TCGPPPMIQF AVQPNLEKMG YDIKNDLLVF

P39866 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