Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nitrate reductase [NAD(P)H]

Gene

NIA1

Organism
Betula pendula (European white birch) (Betula verrucosa)
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(P)+ + H2O = nitrate + NAD(P)H.

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)DescriptionActionsGraphical viewLength
Metal bindingi180MolybdenumBy similarity1
Metal bindingi563Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi586Iron (heme axial ligand)PROSITE-ProRule annotation1

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, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NAD(P)H] (EC:1.7.1.2)
Short name:
NR
Gene namesi
Name:NIA1
OrganismiBetula pendula (European white birch) (Betula verrucosa)
Taxonomic identifieri3505 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFagalesBetulaceaeBetula

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001660751 – 898Nitrate reductase [NAD(P)H]Add BLAST898

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi419InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By nitrate.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP27783.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini528 – 603Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini642 – 754FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST113

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.

P27783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVENRRF THHEPAVNGL VRTFKPVPNS HRSDSPDLGR QIPSSPKKQV
60 70 80 90 100
ATGEDSSSED ENENDYKELI QKGNGELEPS ILDPRDEATA DNWVERNATM
110 120 130 140 150
VRLTGKHPFN SEAPLTRLMH HGFITPAPLH YVRNHGPVPK ARWEDWSVEV
160 170 180 190 200
CGLVKRPARF TMDRLVTEFR SREFPVTLVC AGNRRKEQNM VKKTIGFNWG
210 220 230 240 250
AAGVSTSVWR GVPLRDVLKR CGIFSRGRGA FNVCFEGAED LPGGGGSKYG
260 270 280 290 300
TSVKYEMAMD PARDIILGYM QNGERLSPDH GFPVRMIIPG FIGGRMVKWL
310 320 330 340 350
KRIIVTTKES DNYYHYNDNR VLPSHVDADV AKAEAWWYKP EHIINELNIN
360 370 380 390 400
SVITTPCHEE ILPINSWTTQ RPYTLRGYAY SGGGRKVTRV EITMNGGEKW
410 420 430 440 450
RVCALDHPEK PNKYGKYWCW CFWSLEVEVL DLLGAKEIAV RAWDEAHNTQ
460 470 480 490 500
PEKLIWNVMG MMNNCWFRVK TNVCKAHMGE IGIAFEHPTV PGNESGGWMA
510 520 530 540 550
REKNLETSSD ANQSLKKSVS SPFMNTSSKM FSMSEVKKHN SAESAWIIVH
560 570 580 590 600
GHIYDCTHFL KDHPGGADSI LINAGTDCTE EFDAIHSDKA KKMLEDYRIG
610 620 630 640 650
ELITTGYVSD SPNSTVHGAS NTSHLAPIKE IAPLRNVALI PGAKIPTKLV
660 670 680 690 700
YKKSLSHDVR LFRLALPSDD QVLGLPVGKH VFLCATIDDK LCMRAYTPTS
710 720 730 740 750
TIDEVGYLDL VVKIYFKNSN PRFPNGGLMS QHLDSLPIGS VLHVKGPLGH
760 770 780 790 800
VEYTGRGNFL VHGEPKFAKR LAMVAGGTGI TPIYQVIQAI LKDPEDETEM
810 820 830 840 850
FVVYANRTED DILLREELDD WAKKHEKLKV WYVVKESKRE GWEYSVGYIR
860 870 880 890
ESILREHIPE GSDDVLALAC GAPSMIEEAV RLNLEKMNYD TKNSLIIF
Length:898
Mass (Da):101,002
Last modified:August 1, 1992 - v1
Checksum:iC6B2B2B12FBCDC58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54097 mRNA. Translation: CAA38031.1.
PIRiS15959. RDBJNH.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54097 mRNA. Translation: CAA38031.1.
PIRiS15959. RDBJNH.

3D structure databases

ProteinModelPortaliP27783.
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_BETPN
AccessioniPrimary (citable) accession number: P27783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 5, 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.