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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)DescriptionActionsGraphical viewLength
Metal bindingi137Molybdenum1
Metal bindingi538Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi561Iron (heme axial ligand)PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi829 – 838NADPBy similarity10

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001660441 – 859Nitrate reductase [NADPH]Add BLAST859

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi383InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1859
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 41Combined sources4
Turni44 – 47Combined sources4
Beta strandi54 – 58Combined sources5
Beta strandi63 – 65Combined sources3
Helixi69 – 74Combined sources6
Helixi81 – 83Combined sources3
Beta strandi86 – 90Combined sources5
Helixi97 – 102Combined sources6
Beta strandi104 – 113Combined sources10
Beta strandi115 – 118Combined sources4
Helixi119 – 125Combined sources7
Beta strandi129 – 136Combined sources8
Turni138 – 141Combined sources4
Helixi142 – 148Combined sources7
Beta strandi161 – 170Combined sources10
Helixi171 – 178Combined sources8
Beta strandi186 – 192Combined sources7
Beta strandi201 – 205Combined sources5
Helixi206 – 209Combined sources4
Turni212 – 214Combined sources3
Beta strandi217 – 222Combined sources6
Helixi229 – 231Combined sources3
Turni232 – 234Combined sources3
Beta strandi236 – 238Combined sources3
Helixi244 – 246Combined sources3
Beta strandi249 – 259Combined sources11
Helixi264 – 267Combined sources4
Beta strandi268 – 271Combined sources4
Helixi279 – 284Combined sources6
Helixi286 – 289Combined sources4
Helixi292 – 294Combined sources3
Beta strandi302 – 308Combined sources7
Beta strandi313 – 315Combined sources3
Beta strandi320 – 328Combined sources9
Beta strandi335 – 343Combined sources9
Beta strandi352 – 354Combined sources3
Helixi357 – 362Combined sources6
Beta strandi365 – 368Combined sources4
Beta strandi371 – 373Combined sources3
Helixi375 – 377Combined sources3
Beta strandi385 – 392Combined sources8
Helixi393 – 397Combined sources5
Beta strandi400 – 408Combined sources9
Beta strandi431 – 438Combined sources8
Beta strandi441 – 445Combined sources5
Beta strandi450 – 452Combined sources3
Helixi456 – 462Combined sources7
Turni470 – 473Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP49050.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini502 – 578Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST77
Domaini602 – 713FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST112

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BIHX-ray2.60A19-478[»]
2BIIX-ray1.70A/B59-478[»]
ProteinModelPortaliP49050.
SMRiP49050.
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...

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: November 2, 2016
This is version 106 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.