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Protein

Nitrate reductase [NADH]

Gene

NIA

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activityi

Nitrite + NAD+ + H2O = nitrate + NADH.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • hemeBy similarityNote: Binds 1 heme group per subunit.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041MolybdenumBy similarity
Metal bindingi586 – 5861Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi609 – 6091Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, Molybdenum, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADH] (EC:1.7.1.1)
Short name:
NR
Gene namesi
Name:NIA
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 926926Nitrate reductase [NADH]PRO_0000166071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi443 – 443InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP23312. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP23312.
SMRiP23312. Positions 672-926.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini551 – 62676Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini670 – 782113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the nitrate reductase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR012137. Nitr_rd_NADH.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00173. 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]
PIRSFiPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23312-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVDRQYH PAPMSGVVRT PFSNHHRSDS PVRNGYTFSN PPSSNGVVKP
60 70 80 90 100
GEKIKLVDNN SNSNNGSNNN NNRYDSDSEE DDDENEMNVW NEMIKKGNSE
110 120 130 140 150
LEPSSVDSRD EGTADQWIER NPSMIRLTGK HPFNSEPPLT RLMHHGFLTP
160 170 180 190 200
VPLHYVRNHG PVPNAKWEDW TVEVTGLVKR PIRFTMDQLV NDFQSREFPV
210 220 230 240 250
TLVCAGNRRK EQNMTKQSIG FNWGSAAVST SVWRGVPLRD VLKRCGVMSS
260 270 280 290 300
LKGALNVCFE GAEDLPGGGG SKYGTSVKRE FAMDPARDII LAYMQNGEKL
310 320 330 340 350
SPDHGYPVRM IIPGFIGGRM VKWLKRIIVT TTESDNYYHY KDNRVLPSHV
360 370 380 390 400
DAELANSEAW WYKQEYIINE LNVNSVITSP CHEEILPINA WTTQRPYTMR
410 420 430 440 450
GYAYSGGGRK VTRVEVTMDG GDTWDICELD HQERGSKYGK FWCWCFWSLE
460 470 480 490 500
VEVLDLLGAK EIGVRAWDES LNTQPEKLIW NVMGMMNNCW FRVKTNVCKP
510 520 530 540 550
HKGEIGIVFE HPTQPGNKSG GWMARERHLE ISDSGPTLKR TASTPFMNTT
560 570 580 590 600
SKMYSMSEVK KHNTADSAWI VVHGNVYNAT RFLKDHPGGS DSILINAGTD
610 620 630 640 650
CTEEFDAIHS DKAKRLLEDF RIGELISTGY TSDSSSPGNS VHGGSVYSGL
660 670 680 690 700
AGLAPITEAV PLRNVALNPR VKIPCKLIEK VSLSHDVRRF RFGLPSEDQV
710 720 730 740 750
LGLPVGKHIF LCANVDDKLC MRAYTPSSTI DVVGYFDLVV KVYFKDVHPR
760 770 780 790 800
FPNGGVMSQH LDSLSLGSIV DVKGPLGHIE YLGKGNFTVH GKPKFAKKLA
810 820 830 840 850
MISGGTGITP IYQVMQAILK DPEDKTEMHV VYANRTEEDI LLREELDKWA
860 870 880 890 900
DEFRDRVKVW YVVEKAEEGW KYDTGFISEK ILRDHVPAVG DDVLALTCGP
910 920
PPMIQFAVQP NLDKMGFDIK EQLLIF
Length:926
Mass (Da):103,971
Last modified:November 1, 1991 - v1
Checksum:iFF21DF01963F1AFC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031D → A in BAA13047 (PubMed:9128133).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32600 mRNA. Translation: AAA34033.1.
D86226 Genomic DNA. Translation: BAA13047.1.
U08029 mRNA. Translation: AAA18377.1.
PIRiS11868. RDSPNH.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32600 mRNA. Translation: AAA34033.1.
D86226 Genomic DNA. Translation: BAA13047.1.
U08029 mRNA. Translation: AAA18377.1.
PIRiS11868. RDSPNH.

3D structure databases

ProteinModelPortaliP23312.
SMRiP23312. Positions 672-926.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23312. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR012137. Nitr_rd_NADH.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00173. 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]
PIRSFiPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of a spinach nitrate reductase cDNA."
    Prosser I.M., Lazarus C.M.
    Plant Mol. Biol. 15:187-190(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The nitrate reductase gene isolated from DNA of cultured spinach cells."
    Tamura N., Takahashi H., Takeba G., Satoi T., Nakagawa H.
    Biochim. Biophys. Acta 1338:151-155(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Hoyo.
  3. "Sequence analysis of cloned cDNA and proteolytic fragments for nitrate reductase from Spinacia oleracea L."
    Shiraishi N., Kubo Y., Takeba K., Kiyota S., Sakano K., Nakagawa H.
    Plant Cell Physiol. 32:1031-1038(1991)
    Cited for: NUCLEOTIDE SEQUENCE OF 287-926.
    Strain: cv. Hoyo.

Entry informationi

Entry nameiNIA_SPIOL
AccessioniPrimary (citable) accession number: P23312
Secondary accession number(s): Q41377
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 6, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.