[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Saxa; TISSUE=Shoot; Hoff T., Stummann B.M., Henningsen K.W.; "Cloning and expression of a gene encoding a root specific nitrate reductase in bean (Phaseolus vulgaris)."; Physiol. Plantarum 82:197-204(1991).

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

X53603; CAA37672.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S25445; S25445.

3D structure databases

HSSP

P17571; 2CND. [HSSP ENTRY / PDB]

ModBase

P39865.

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`	`1 881`	`881`	`Nitrate reductase [NADH] 1.`	`PRO_0000166067`
`DOMAIN`	`515 590`	`76`	`Cytochrome b5 heme-binding.`
`DOMAIN`	`625 737`	`113`	`FAD-binding FR-type.`
`METAL`	`167 167`		`Molybdenum-pterin (Potential).`
`METAL`	`221 221`		`Molybdenum-pterin (Potential).`
`METAL`	`550 550`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`573 573`		`Iron (heme axial ligand) (By similarity).`
`DISULFID`	`406 406`		`Interchain (Potential).`

Sequence information

Length: 881 AA [This is the length of the unprocessed precursor]

Molecular weight: 99223 Da [This is the MW of the unprocessed precursor]

CRC64: A212A1288B4EE661 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAASVEHRPF TSHQHGVVRS FKSYPDVPRP KKLPLPQPLS DSTNDNDEEA AVWKELVLKS 

        70         80         90        100        110        120 
SAGVEPSIFD PRDDGTSDQW IKRNASMIRL TGKHPFNAEP PLPRLMQHGF ITPSPIHYVR 

       130        140        150        160        170        180 
SHGPVPHARW EDWTVEVTGL VTRPTCFTME QLVNDFPSHE FPATLVCAGN RRKEQNMVKQ 

       190        200        210        220        230        240 
SIGFNWGAGG VSTSVWRGVS LRSLLKRCGI YSRAKGALHV CFEGAEDLPG GGGSNYGTSL 

       250        260        270        280        290        300 
MREVALDPSR DIILAYMQNG ELLSPDHGFP VRMIIPGFIG GRMVKWLKRI VVSNQQSQSH 

       310        320        330        340        350        360 
YHYKDNKLFP SHVDAELANE EDWWYKPEYI INEVNINSVI TTPSHQEILP INSWTTQMPY 

       370        380        390        400        410        420 
SMRGYAYSGG GRKVTRVEVT LDGGETWQVC SVERLEKPNK YGKYWCWCFW SLEVEVLDIL 

       430        440        450        460        470        480 
GAKEIAVRAW DEAQNTQPEK LIWNTMGMIN NCWFRVKTNV CKPKKGEIGI VFEHPTQPGN 

       490        500        510        520        530        540 
QSGGWMAREK QLEKSSESNP ILKKSVSSPF MNTATKSYSL SEVRRHNNRD SAWIIVNGHV 

       550        560        570        580        590        600 
YDCTRFLKDH PGGEDSILLN AGTDCTEEFE AIHSDKAKKM LEDYRIGELM TTDYTSDSSS 

       610        620        630        640        650        660 
SNNSVHGNSE TTHLAPIREV ALNPREKIPC KLLSKTSISH DVRLLRFALP AEDQVMGLPV 

       670        680        690        700        710        720 
GNHVFLCATV DEKLCMRAYT PTSSVDEVGF FDLVVKVYFK GVHPNFPNGG IMSQHLDSLP 

       730        740        750        760        770        780 
IGSVVDVKGP LGHIEYTGRG NFLVHGKPRF AKRLTMLAGG TGITPIYQVV QAILKDPEDR 

       790        800        810        820        830        840 
TEMYVVYANR TEDDILLKEE LDEWAKKHDR LKVWYVLQAN IREGWEYSVG FITESILREH 

       850        860        870        880 
VPLASPDTLA LTCGPPPMIQ FAVQPNLEKL GYDIQNDLLV F

P39865 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