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Protein

Nitrate reductase [NADH]

Gene

NIA

Organism
Cichorium intybus (Chicory)
Status
Reviewed-Annotation score: Annotation score: 3 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 bindingi185 – 1851MolybdenumBy similarity
Metal bindingi569 – 5691Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi592 – 5921Iron (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
OrganismiCichorium intybus (Chicory)
Taxonomic identifieri13427 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeCichorioideaeCichorieaeCichoriinaeCichorium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 920920Nitrate reductase [NADH]PRO_0000166054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi424 – 424InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

In cortical cells of roots grown at low nitrate concentrations, in vascular tissues of roots at high nitrate concentrations and in root apex under both conditions.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP43101.
SMRiP43101. Positions 665-920.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini534 – 60976Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini663 – 775113FAD-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.

P43101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVENRQF RHEPGLSAAG VVRSFSPNHR RSDSPIRNCN YPAAAREFMT
60 70 80 90 100
PKKLPPETYD TSDDEEDEAD YRDAIKKSNS ELESSVFDPR DQGTADQWIE
110 120 130 140 150
RNPSMVRLTG KHPFNSEPPL NKLMQHGFIT PDPLHYVRNH GPVPNATWED
160 170 180 190 200
WTVEICGLVK RPARFSMTQL VNEFPSREFP VTLVCAGNRR KEQNLTKQTI
210 220 230 240 250
GFNWGAAGIS TSVWKGVPLV HILKRCGIYS RKKGALNVCF EGAEDLPGGG
260 270 280 290 300
GSKYGTSIKI EMAMDPARDI ILAYMQNGEK LSPDHGFPVR MIIPGFIGGR
310 320 330 340 350
MVKWLKRIIV TTPESESYYH FKDNRVLPSH VDAELANSEG WWYKPEYIIN
360 370 380 390 400
ELNINSVITT PCHEEILPIN SWTTQRPYTL RGYAYSGGGK KVTRVEVTMD
410 420 430 440 450
GGETWNVCTL DHKEKPTRYA KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE
460 470 480 490 500
TLNTQPDKLI WNLMGMMNNC WFRVKTNMCK PHKGEIGIVF EHPTQPGNQS
510 520 530 540 550
GGWMAREKHL EISSELAHPT LKKSVSSPFM NTTSLTFTMS EVKKHNSADS
560 570 580 590 600
AWIVVHGHIY DCTSFLKDHP GGSDSILLNA GTDCTEEFDA IHSDKAKKLL
610 620 630 640 650
EEYRVGELIT MGYSSDSAAS SPNNSVHGAT NYLTLHLSLA TIKEIAPTRS
660 670 680 690 700
VALIPKEIAP TRREKIPCKL ISKTSVSHDV RLFRFALPSP DQVLGLPVGK
710 720 730 740 750
HVFVCATIDD KLCMRAYTPT STIDEVGYFE LLVKIYFKGV EPKFPNGGLM
760 770 780 790 800
SQHLESMELG SSIEIKGPLG HIEYMGRGTF SVHGKQKFAR KLAMFAGGTG
810 820 830 840 850
ITPDLSSDAS YLKDPEDDTE MYVVYANRTE DDILLREELD AWADKYSDRV
860 870 880 890 900
KVWYVVAKSI REGWKYSEGF ITEDIMREHV PEVSEDTLAL ACGPPPMIQF
910 920
AINPNLEKMG YDIKNSLLVF
Length:920
Mass (Da):103,520
Last modified:November 1, 1995 - v1
Checksum:iFE1E332CCC9A4D58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84103 Genomic DNA. Translation: CAA58909.1.
X84102 mRNA. Translation: CAA58908.1.
PIRiS52301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84103 Genomic DNA. Translation: CAA58909.1.
X84102 mRNA. Translation: CAA58908.1.
PIRiS52301.

3D structure databases

ProteinModelPortaliP43101.
SMRiP43101. Positions 665-920.
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...

Entry informationi

Entry nameiNIA_CICIN
AccessioniPrimary (citable) accession number: P43101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 94 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.