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Protein

Nitrate reductase [NADPH]

Gene

YNR1

Organism
Pichia angusta (Yeast) (Hansenula polymorpha)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activityi

Nitrite + NADP+ + H2O = nitrate + NADPH.

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-molybdopterin1 PublicationNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi137 – 1371Molybdenum
Metal bindingi538 – 5381Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi561 – 5611Iron (heme axial ligand)PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi829 – 83810NADPBy similarity

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, NADP

Enzyme and pathway databases

BRENDAi1.7.1.3. 2587.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADPH] (EC:1.7.1.3)
Short name:
NR
Gene namesi
Name:YNR1
OrganismiPichia angusta (Yeast) (Hansenula polymorpha)
Taxonomic identifieri870730 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataea

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Nitrate reductase [NADPH]PRO_0000166044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi383 – 383InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
859
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 414Combined sources
Turni44 – 474Combined sources
Beta strandi54 – 585Combined sources
Beta strandi63 – 653Combined sources
Helixi69 – 746Combined sources
Helixi81 – 833Combined sources
Beta strandi86 – 905Combined sources
Helixi97 – 1026Combined sources
Beta strandi104 – 11310Combined sources
Beta strandi115 – 1184Combined sources
Helixi119 – 1257Combined sources
Beta strandi129 – 1368Combined sources
Turni138 – 1414Combined sources
Helixi142 – 1487Combined sources
Beta strandi161 – 17010Combined sources
Helixi171 – 1788Combined sources
Beta strandi186 – 1927Combined sources
Beta strandi201 – 2055Combined sources
Helixi206 – 2094Combined sources
Turni212 – 2143Combined sources
Beta strandi217 – 2226Combined sources
Helixi229 – 2313Combined sources
Turni232 – 2343Combined sources
Beta strandi236 – 2383Combined sources
Helixi244 – 2463Combined sources
Beta strandi249 – 25911Combined sources
Helixi264 – 2674Combined sources
Beta strandi268 – 2714Combined sources
Helixi279 – 2846Combined sources
Helixi286 – 2894Combined sources
Helixi292 – 2943Combined sources
Beta strandi302 – 3087Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi320 – 3289Combined sources
Beta strandi335 – 3439Combined sources
Beta strandi352 – 3543Combined sources
Helixi357 – 3626Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi371 – 3733Combined sources
Helixi375 – 3773Combined sources
Beta strandi385 – 3928Combined sources
Helixi393 – 3975Combined sources
Beta strandi400 – 4089Combined sources
Beta strandi431 – 4388Combined sources
Beta strandi441 – 4455Combined sources
Beta strandi450 – 4523Combined sources
Helixi456 – 4627Combined sources
Turni470 – 4734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BIHX-ray2.60A19-478[»]
2BIIX-ray1.70A/B59-478[»]
ProteinModelPortaliP49050.
SMRiP49050. Positions 24-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49050.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini502 – 57877Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini602 – 713112FAD-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.

P49050-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSIVTEVTY GLEIKKIKDI TELPFPVRQD SPLTEVLPTD LKTKDNFVAR
60 70 80 90 100
DPDLLRLTGS HPFNSEPPLT KLYDSGFLTP VSLHFVRNHG PVPYVPDENI
110 120 130 140 150
LDWEVSIEGM VETPYKIKLS DIMEQFDIYS TPVTMVCAGN RRKEQNMVKK
160 170 180 190 200
GAGFNWGAAG TSTSLWTGCM LGDVIGKARP SKRARFVWME GADNPANGAY
210 220 230 240 250
RTCIRLSWCM DPERCIMIAY QQNGEWLHPD HGKPLRVVIP GVIGGRSVKW
260 270 280 290 300
LKKLVVSDRP SENWYHYFDN RVLPTMVTPE MAKSDDRWWK DERYAIYDLN
310 320 330 340 350
LQTIICKPEN QQVIKISEDE YEIAGFGYNG GGVRIGRIEV SLDKGKSWKL
360 370 380 390 400
ADIDYPEDRY REAGYFRLFG GLVNVCDRMS CLCWCFWKLK VPLSELARSK
410 420 430 440 450
DILIRGMDER MMVQPRTMYW NVTSMLNNWW YRVAIIREGE SLRFEHPVVA
460 470 480 490 500
NKPGGWMDRV KAEGGDILDN NWGEVDDTVK QAERRPHIDE DLEMMCNREK
510 520 530 540 550
MDVVIKYSEF EAHKDSETEP WFAVKGQVFD GSSYLEDHPG GAQSILMVSG
560 570 580 590 600
EDATDDFIAI HSSFAKKLLP SMHLGRLEEV SSVTKVKSVE QNVKREVLLD
610 620 630 640 650
PRKWHKITLA EKEVISSDSR IFKFDLEHSE QLSGLPTGKH LFLRLKDSSG
660 670 680 690 700
KYVMRAYTPK SSNSLRGRLE ILIKVYFPNR EYPNGGIMTN LIENLQVGNQ
710 720 730 740 750
IEVKGPVGEF EYVKCGHCSF NNKPYQMKHF VMISGGSGIT PTYQVLQAIF
760 770 780 790 800
SDPEDRTSVQ LFFGNKKVDD ILLREELDHI QEKYPEQFKV DYSLSDLDHL
810 820 830 840 850
PENWSGVRGR LTFDILDTYV RGKKMGEYML LVCGPPGMNG VVENWCNARK

LDKQYVVYF
Length:859
Mass (Da):98,534
Last modified:February 1, 1996 - v1
Checksum:i79569977B01E3967
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49110 Genomic DNA. Translation: CAA88925.1.
PIRiS65938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49110 Genomic DNA. Translation: CAA88925.1.
PIRiS65938.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BIHX-ray2.60A19-478[»]
2BIIX-ray1.70A/B59-478[»]
ProteinModelPortaliP49050.
SMRiP49050. Positions 24-476.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.7.1.3. 2587.

Miscellaneous databases

EvolutionaryTraceiP49050.

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. "Cloning and disruption of the YNR1 gene encoding the nitrate reductase apoenzyme of the yeast Hansenula polymorpha."
    Avila J., Perez M.D., Brito N., Gonzalez C., Siverio J.M.
    FEBS Lett. 366:137-142(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL Y-1798 / VKM Y-1397.
  2. "Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site."
    Fischer K., Barbier G.G., Hecht H.J., Mendel R.R., Campbell W.H., Schwarz G.
    Plant Cell 17:1167-1179(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-478 IN COMPLEX WITH MO-MOLYBDOPTERIN, COFACTOR, SUBUNIT, REACTION MECHANISM.

Entry informationi

Entry nameiNIA_PICAN
AccessioniPrimary (citable) accession number: P49050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.