NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. TLRL13;
TISSUE=Leaf;
DOI=10.1016/0378-1119(93)90557-J; PubMed=8514183 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Ha D.B.D.;
"Analysis of the petunia nitrate reductase apoenzyme-encoding gene: a first step for sequence modification analysis.";
Gene 128:147-154(1993).

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.
COFACTOR: Binds 1 heme group per subunit.
COFACTOR: Binds 1 molybdenum-pterin group per subunit.
ENZYME REGULATION: Regulated by the nitrogen source and controlled by the circadian rhythm.
SUBUNIT: Homodimer (By similarity).
DEVELOPMENTAL STAGE: Maximum expression 2 hours after sunrise. Low expression found 2 hours before and 8 hours after sunrise.
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

L13691; AAA33713.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P36859.

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`	`1 909`	`909`	`Nitrate reductase [NADH].`	`PRO_0000166066`
`DOMAIN`	`535 610`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`652 764`	`113`	`FAD-binding FR-type.`
`METAL`	`187 187`		`Molybdenum-pterin (Potential).`
`METAL`	`241 241`		`Molybdenum-pterin (Potential).`
`METAL`	`570 570`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`593 593`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`426 426`		`Interchain (Potential).`

Sequence information

Length: 909 AA [This is the length of the unprocessed precursor]

Molecular weight: 102376 Da [This is the MW of the unprocessed precursor]

CRC64: 502C706F6E63E706 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVENRQF SHLEPGLSGV VRSFKPRSDS PVRGCNFPLN NELTNFQKKP NTTIYLDCSS 

        70         80         90        100        110        120 
SEDDDDDDDK NEYLQMIRKG KLEVEPSVHD IRDEGTADNW IERNNSMIRL TGKHPFNSEP 

       130        140        150        160        170        180 
PLARLMHHGF ITPVPLHYVR NHGPVPKGMW DDWTVEVTGL VKRPMKFTME QLVNEFPSRE 

       190        200        210        220        230        240 
LPVTLVCAGN RRKEQNMVKQ TIGFNWGAAA VSTTVWRGVP LRAILKRCGI YSRTKGALNI 

       250        260        270        280        290        300 
CFEGADVLPG GGGSKYGTSI KKEFAMDPSR DIIIAYMQNG EKLTPDHGFP LRMIIPGFIG 

       310        320        330        340        350        360 
GRMVKWLKRI IVTTQESESY YHYKDNRVLP PHVDAELANA EAWWYKPEYI INELNINSVI 

       370        380        390        400        410        420 
TTPCHEEILP INSWTTQRPY TLRGYSYSGG GKKVTRVEVT MDGGETWNVC TVDHPEKPNK 

       430        440        450        460        470        480 
YGKYWCWCFW SLEVEVLDLL SAKEIAVRAW DETLNTQPEK LIWNVMGMMN NCWFRVKTNV 

       490        500        510        520        530        540 
CKPHKGEIGI VFEHPTQPGN LSGGWMAKER HLEISAEAPP TLKKSISTPF MNTASKMYSM 

       550        560        570        580        590        600 
SEVKKHNSAD SAWIIVHGHV YDATRFLKDH PGGIDSILIN AGTDCTEEFD AIHSDKAKKL 

       610        620        630        640        650        660 
LEDFRIGELI TTGYTSDSSP NNSVHGSSSF SGFLAPIKEL APAVRSVALI PREKIPCKLV 

       670        680        690        700        710        720 
DKKSISHDVR KFRFALPSED QVLGLPVGKH IFLCAIIDDK LCMRAYTPTS TVDEVGYFEL 

       730        740        750        760        770        780 
VVKIYFKGIV PKFPNGGQMS QYLDSLPLGA FVDVKGPLGH IEYQGRGNFL VHGKRKFAKK 

       790        800        810        820        830        840 
LAMLAGGTGI TPVYQVMQAI LKDPEDETEM HVVYANRTED DILLKDELDS WAVKLPERVK 

       850        860        870        880        890        900 
VWYVVQDSIK EGWKYSTGFI TEAVLREHIP LPSQTTLALA CGPPPMIQFA VNPNLEKMGY 


DIKDSLLVF

P36859 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