[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. B73; TISSUE=Seedling; Campbell W.H., Redinbaugh M.G., Ingemarsson B., Doughtery E.S., Campbell E.R.; Submitted (JAN-1995) 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 per subunit (By similarity).
COFACTOR: Binds 1 heme group per subunit (By similarity).
COFACTOR: Binds 1 molybdenum-pterin group per subunit (By similarity).
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

U20450; AAA62316.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T02240; T02240.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

SMR

P49102; 632-889.

ModBase

P49102.

Organism-specific databases

Gramene

P49102; -.

MaizeGDB

30041; -.

Ontologies

GO:0009703;	Molecular function: nitrate reductase (NADH) 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; NAD; Nitrate assimilation; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 889`	`889`	`Nitrate reductase [NADH] 3.`	`PRO_0000166064`
`DOMAIN`	`520 595`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`630 742`	`113`	`FAD-binding FR-type.`
`METAL`	`181 181`		`Molybdenum-pterin (Potential).`
`METAL`	`235 235`		`Molybdenum-pterin (Potential).`
`METAL`	`555 555`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`578 578`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`404 404`		`Interchain (Potential).`

Sequence information

Length: 889 AA [This is the length of the unprocessed precursor]

Molecular weight: 98811 Da [This is the MW of the unprocessed precursor]

CRC64: 3614A8BB44B822F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTCVEQPTH SASLDPTAAQ RLPYPDLPVD ILRRSSVRGS GFVAAALVSS ARKADDDARH 

        70         80         90        100        110        120 
DDDDPSGDRH ETYGSHYLAN LGVEQSVRDE GTVDAWVESS QSLIRLTGKH SLNGELPRLM 

       130        140        150        160        170        180 
RHGFITPVPR HYVRNHGPVP RGDWATWTVE VTGLVRRPRA LTMDELARDF PALELPVTLV 

       190        200        210        220        230        240 
CAGNRRKEQN MVRQTLGFNW GPGAVSTSVW RGARLSDVLR RCGSMSRKGG ALFVCFEGAE 

       250        260        270        280        290        300 
DLPGGGGTKY GTSITREVAL DPTMDVMLAY QQNGGPLLPD HGFPVRLIVP GCTAGRMVKW 

       310        320        330        340        350        360 
LKRIVVAPAE SDNYYHYRDN RFLPSHVDAK LADAEGWWYK PEYVINEMNT NSVITTPAHN 

       370        380        390        400        410        420 
EFLPINAITT QRIYTMKGFA YSGGGKKVTR VEVTLDGGEN WLLCELDHPE KPTKYGRYWC 

       430        440        450        460        470        480 
WCFWSIDVEL IDLLACKEIA VRAWDQSLNT QPEFLTWNLM GMMTNCWFRV KVNVCRPRHG 

       490        500        510        520        530        540 
EKAGLAFEHP VRTNQPGGWM AQQKHLETAE RTSAATSTTN QQFTMSEVRK HASQDSAWIV 

       550        560        570        580        590        600 
VHGHVYDCTA FLKDHPGGAD SILINAGTDC TEEFDAIHSD KAKELLDTYR IGDLVTTGGA 

       610        620        630        640        650        660 
EQRSPLELAP SPPIRHEGPA APVIALSNPR EKVPCQLVAR TVLSRDVRLF RFALPSSGQV 

       670        680        690        700        710        720 
LGLPVGKHIF VCASIDGKLC MRAYTPTSSV DEVGHFDLLV KVYFRNENTK FPDGGRMTQY 

       730        740        750        760        770        780 
LDSLPVGAHV DVKGPLGHVE YVGRGGFVID GKPRKAGRLA MVAGGSGITP IYQVIQAVLR 

       790        800        810        820        830        840 
DQPEDKTEMH LVYANRTEDD ILLRAELDRW AAEYPERLKV WYVVSQVKRL DEWKYSVGIV 

       850        860        870        880 
TEAVLRDDVP EARDGTLALL CGPPSMIQSP ILPNLEKMKH QLDDSVVSF

P49102 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