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Protein

Nitrate reductase [NADH] 1

Gene

NIA1

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi183MolybdenumBy similarity1
Metal bindingi566Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi589Iron (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

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADH] 1 (EC:1.7.1.1)
Short name:
NR1
Gene namesi
Name:NIA1
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001660721 – 904Nitrate reductase [NADH] 1Add BLAST904

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi422InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP11605.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini531 – 606Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini647 – 759FAD-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.

P11605-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVENRQF SHIEAGLSRS FKPRSDSPVR GCNFPPPNST NFQKKPNSTI
60 70 80 90 100
FLDYSSSEDD DDDDEKNEYL QMIKKGNSEL EPSVHDSRDE GTADNWIERN
110 120 130 140 150
FSLIRLTGKH PFNSEPPLNR LMHHGFITPV PLHYVRNHGP VPKGTWDDWT
160 170 180 190 200
VEVTGLVKRP MKFTMDQLVN EFPSRELPVT LVCAGNRRKE QNMVKQTIGF
210 220 230 240 250
NWGAAAVSTT VWRGVPLRAL LKRYGVFSKN KGALNVCFEG ADVLPGGGGS
260 270 280 290 300
KYGTSIKKEF AMDPARDIII AYMQNGEKLA PDHGFPVRMI IPGFIGGRMV
310 320 330 340 350
KWIKRIIVTT QESDSYYHFK DNRVLPPHVD AELANTEAWW YKPEYIINEL
360 370 380 390 400
NINSVITTPC HEEILPINAW TTQRPYTLRG YSYSGGGKKV TRVEVTLDGG
410 420 430 440 450
ETWQVCTLDH PEKPTKYGKY WCWCFWSLEV EVLDLLSAKE IAVRAWDETL
460 470 480 490 500
NTQPEKLIWN VMGMMNNCWF RVKMNVCKPH KGEIGIVFEH PTQPGNQSGG
510 520 530 540 550
WMAKERHLEI SAEAPPTLKK SISTPFMNTA SKMYSMSEVR KHSSADSAWI
560 570 580 590 600
IVHGHIYDAT RFLKDHPGGS DSILINAGTD CTEEFDAIHS DKAKKLLEEF
610 620 630 640 650
RIGELLTTGY TSDSPGNSVH GSSSFSSFLA PIKELVPAQR SVALIPREKI
660 670 680 690 700
PCKLIDKQSI SPDVRKFRFA LPSEDQVLGL PVGKHIFLCA VIDDKLCMRA
710 720 730 740 750
YTPTSTIDEV GYFELVVKIY FKGIHPKFPN GGQMSQYLDS LQLGSFLDVK
760 770 780 790 800
GPLGHIEYQG KGNFLVHGKQ KFAKKLAMIA GGTGITPVYQ VMQAILKDPE
810 820 830 840 850
DDTEMYVVYA NRTEDDILLK EELDSWAEKI PERVKVWYVV QDSIKEGWKY
860 870 880 890 900
SLGFISEAIL REHIPEPSHT TLALACGPPP MIQFAVNPNL EKMGYDIKDS

LLVF
Length:904
Mass (Da):101,908
Last modified:October 1, 1989 - v1
Checksum:i85642BDA723EE154
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14058 Genomic DNA. Translation: CAA32216.1.
PIRiS04838. RDNTNT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14058 Genomic DNA. Translation: CAA32216.1.
PIRiS04838. RDNTNT.

3D structure databases

ProteinModelPortaliP11605.
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 nameiNIA1_TOBAC
AccessioniPrimary (citable) accession number: P11605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 5, 2016
This is version 104 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.