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Protein

Nitrate reductase [NADH]

Gene
N/A
Organism
Cucurbita maxima (Pumpkin) (Winter squash)
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 bindingi195 – 1951MolybdenumBy similarity
Metal bindingi578 – 5781Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi601 – 6011Iron (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
OrganismiCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifieri3661 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Nitrate reductase [NADH]PRO_0000166055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi434 – 434InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By nitrate.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP17569.
SMRiP17569. Positions 663-918.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini543 – 61876Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini661 – 774114FAD-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.

P17569-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVDNRQY GPLQPPLSGV VRSFKNGPNH RADSPVRGCN FPNSNVDYNN
60 70 80 90 100
NRPLKSSVKI QEAAAEEMED SCSEDENENE FRDLIVKGNR ELEPSILDHR
110 120 130 140 150
DEGTADNWIE RNASMVRLTG KHPFNSEPPL NRLMHHGFIT PVPLHYVRNH
160 170 180 190 200
GVVPKAKWAD WTVEVCGLVK RPAKFTMDQL LNEFRFREFP ATLVCAGNRR
210 220 230 240 250
KEQNMVKQSI GFNWGAAGVS TSVWRRVPLC DLLKRCGILS RKKGALNVCF
260 270 280 290 300
EGAEDLPGGG GSKYGTSIKK ELAMDPARDI ILAYMQNGEQ LAPDHGFPVR
310 320 330 340 350
MIIPGFIGGR MVKWLKRIIV TTKESENYYH FKDNRVLPSH VDADVANAEA
360 370 380 390 400
WWYKPEHIIN ELNINSVITT PCHEEILPIN AWTTQRPYTL RGYSYSGGGK
410 420 430 440 450
KVTRVEVTMD SGETWQVCTL DHPEKANKYG KYWCWCFWSL EVEVLDLLSA
460 470 480 490 500
KEIAVRAWDE THNTQPEKLI WNLMGMMNNC WFRVKTNMCK PHKGEIGIVF
510 520 530 540 550
EHPTQPGNQS GGWMDRERHL EISTESNQTL KKSVSTPFMN TASNTYTLSE
560 570 580 590 600
VKKHNSPQSA WIIVHGHVYD CTRFLKDHPG GSDSILINAG TDCTEEFDAI
610 620 630 640 650
HSDKAKKMLE DYRIGELITT GYASDSSSNS PNNSTHGASN FSHLAPIREA
660 670 680 690 700
PVSRRVALAP NEKIPCKLIS KTSISHDVRV FRFALPGGQD QALGLPVGKH
710 720 730 740 750
IFICATVDGK LCMRAYTPTS SIDEMGFFEL VVKVYFKGVH PKFPNGGIMS
760 770 780 790 800
QYLDSMEVGS TLDVKGPLGH IEYTGRGNFM VHGKPRFARR LAMLAGGTGI
810 820 830 840 850
TPIYQVVQAI LKDPEDETEM YVVYANRTED DILLRDELDT WAKKNQRLKV
860 870 880 890 900
WYVVQESIRE GWEYSVGFIT ENILREHIPA AAEDTLALAC GPPAMIQFAV
910
QPNLEKMNYD TKNSLLVF
Length:918
Mass (Da):103,384
Last modified:August 1, 1990 - v1
Checksum:iA2CAFDDADEA1B2D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33154 mRNA. Translation: AAA33114.1.
PIRiA41667.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33154 mRNA. Translation: AAA33114.1.
PIRiA41667.

3D structure databases

ProteinModelPortaliP17569.
SMRiP17569. Positions 663-918.
ModBaseiSearch...
MobiDBiSearch...

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. "Nitrate reductase from squash: cDNA cloning and nitrate regulation."
    Crawford N.M., Campbell W.H., Davis R.
    Proc. Natl. Acad. Sci. U.S.A. 83:8073-8076(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases."
    Hyde G.E., Crawford N.M., Campbell W.H.
    J. Biol. Chem. 266:23542-23547(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Seedling.

Entry informationi

Entry nameiNIA_CUCMA
AccessioniPrimary (citable) accession number: P17569
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 11, 2016
This is version 100 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.