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Reviewed, UniProtKB/Swiss-Prot P36859 (NIA_PETHY)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nitrate reductase [NADH]
      Short name=NR
    EC=1.7.1.1
Gene names
Name: NIA
OrganismPetunia hybrida (Petunia)
Taxonomic identifier4102 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

Protein attributes

Sequence length909 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (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.

Binds 1 heme group per subunit.

Binds 1 molybdenum-pterin group per subunit.

Enzyme regulation

Regulated by the nitrogen source and controlled by the circadian rhythm.

Subunit structure

Homodimer By similarity.

Developmental stage

Maximum expression 2 hours after sunrise. Low expression found 2 hours before and 8 hours after sunrise.

Sequence similarities

Belongs to the nitrate reductase family.

Contains 1 cytochrome b5 heme-binding domain.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 909909Nitrate reductase [NADH]
PRO_0000166066

Regions

Domain535 – 61076Cytochrome b5 heme-binding
Domain652 – 764113FAD-binding FR-type

Sites

Metal binding1871Molybdenum-pterin Potential
Metal binding2411Molybdenum-pterin Potential
Metal binding5701Iron (heme axial ligand) By similarity
Metal binding5931Iron (heme axial ligand) By similarity

Amino acid modifications

Disulfide bond426Interchain Potential

Sequences

Sequence LengthMass (Da)Tools
P36859-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 502C706F6E63E706

FASTA909102,376
        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 

« Hide

References

[1]"Analysis of the petunia nitrate reductase apoenzyme-encoding gene: a first step for sequence modification analysis."
Salanoubat M., Ha D.B.D.
Gene 128:147-154(1993) [PubMed: 8514183] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. TLRL13.
Tissue: Leaf.

Cross-references

Sequence databases

L13691 Genomic DNA. Translation: AAA33713.1.

3D structure databases

HSSPHSSP built from PDB template 2CND based on UniProtKB P17571.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.7.1.1. 2263.

Family and domain databases

InterProIPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR012137. Nitr_rd_NADH.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR000572. OxRdtase_Mopterin-bd.
[Graphical view]
Gene3DG3DSA:3.10.120.10. Cyt_B5. 1 hit.
G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit.
G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.
PfamPF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PIRSFPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
ProDomPD000612. Cyt_B5. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNIA_PETHY
AccessionPrimary (citable) accession number: P36859
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents