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Protein

Nitrate reductase [NADH], clone PBNBR1405

Gene

NIA1

Organism
Brassica napus (Rape)
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.By similarity
  • hemeBy similarityNote: Binds 1 heme group. The heme group is called cytochrome b-557.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi191 – 1911MolybdenumBy similarity
Metal bindingi574 – 5741Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi597 – 5971Iron (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], clone PBNBR1405 (EC:1.7.1.1)
Short name:
NR
Gene namesi
Name:NIA1
OrganismiBrassica napus (Rape)
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Nitrate reductase [NADH], clone PBNBR1405PRO_0000166051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi430 – 430InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP39867.
SMRiP39867. Positions 656-911.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini539 – 61476Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini654 – 766113FAD-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

Phylogenomic databases

KOiK10534.

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.

P39867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSVDNRHY PRLSSALNGG VVHSFKPPLV PSPSLDRDQD QSVNVPTEKS
60 70 80 90 100
VDKTTKEDRF DSSDDEDESH NRYVSYYKEM VLKSNSDLEP TALDSRDEST
110 120 130 140 150
GDKWIHRNSS MVRLTGKHPF NAEAPLPRLM HHGFITPVPL HYVRNHGGVP
160 170 180 190 200
KAEWSDWSVE VTGLVKRPAG LTMEQLISEF PSREFPVTLV CAGNRRKEQN
210 220 230 240 250
MVKQTIGFNW GSAGVSTSLW RGVALSDVLR RCGVYSKRGG ALNVCFEGAE
260 270 280 290 300
DLPGGGGSKY GTSIKKEMAM DPARDIILAY MQNGELLTPD HGFPVRVIIP
310 320 330 340 350
GFIGGRMVKW LKRIIVTPQE SDNYYHYKDN RVLPSYVDAE LPNEESWWYR
360 370 380 390 400
PEYIINELNI NSVITTPGHE EILPINAFTT QKPYTLKGYA YSGGGKKVTR
410 420 430 440 450
VEVTLDGGET WSVCELDHQE KPNKYGKFWC WCFWSLDVEV LDLLSAKEVA
460 470 480 490 500
VRAWDESLNT QPEKLIWNLM GMMNNCWFRI KTNVCKPHRG EIGIVFEHPT
510 520 530 540 550
RPGNQSGGWM AKERQIEKSS ESHPTLKKSV STPFMNTASK MYSMSEVRKH
560 570 580 590 600
NSAESAWIIV HGHIYDCTRF LKDHPGGSDS ILINAGTDCT EEFEAIHSDK
610 620 630 640 650
AKKLLEDYRI GELITTGYDS SPNVSVHGGS SVMSLLAPIR QLAPTKNIAL
660 670 680 690 700
VNPREKVPVK LIEKTSISHD VRRFRFALPS EDQQLGLPVG KHIFLCATIN
710 720 730 740 750
DKLCLRAYTP TSTVDAVGYI DLVIKVYFKN VHPRFPNGGL MSQHPDSLPI
760 770 780 790 800
GAVLDIKGPL GHIEYQGRGK FMVSGKPKFA NKLAMLAGGT GITPIYQVIQ
810 820 830 840 850
SILSDPEDET EMFVVYANRT EDDILVREEL EGWASKFPDR LKIWYVVEIA
860 870 880 890 900
KEGWEYSTGF ITEAVLREHV PEGLEGESLA LACGPPPMIQ FALQPNLEKM
910
GYDIKEDLLI F
Length:911
Mass (Da):102,252
Last modified:February 1, 1995 - v1
Checksum:iBBA4E19835B03D8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38219 mRNA. Translation: BAA07394.1.
PIRiT08105.
RefSeqiNP_001302849.1. NM_001315920.1.
UniGeneiBna.2265.

Genome annotation databases

GeneIDi106400358.
KEGGibna:106400358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38219 mRNA. Translation: BAA07394.1.
PIRiT08105.
RefSeqiNP_001302849.1. NM_001315920.1.
UniGeneiBna.2265.

3D structure databases

ProteinModelPortaliP39867.
SMRiP39867. Positions 656-911.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi106400358.
KEGGibna:106400358.

Phylogenomic databases

KOiK10534.

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. "Developmental stage-specific and nitrate-independent regulation of nitrate reductase gene expression in rapeseed."
    Fukuoka H., Ogawa T., Minami H., Yano H., Ohkawa Y.
    Plant Physiol. 111:39-47(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Lisandra.

Entry informationi

Entry nameiNIA1_BRANA
AccessioniPrimary (citable) accession number: P39867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 99 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.