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Protein

Inositol-pentakisphosphate 2-kinase

Gene

IPK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). Phytate is a regulator of intracellular signaling, a highly abundant animal antinutrient, and a phosphate store in plant seeds. Also phosphorylates Ins(1,3,4,6)P4 and Ins(1,4,5,6)P4 to produce Ins(1,2,3,4,6)P5 and Ins(1,2,4,5,6)P5.2 Publications

Catalytic activityi

ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol hexakisphosphate.2 Publications

Cofactori

Zn2+4 PublicationsNote: Binds 1 zinc ion per subunit.4 Publications

Kineticsi

  1. KM=38 µM for Ins(1,3,4,5,6)P5 (in the presence of 0.4 mM ATP)1 Publication
  2. KM=176 µM for Ins(1,3,4,5,6)P5 (in the presence of 0.4 µM ATP)1 Publication
  1. Vmax=22 nmol/min/mg enzyme (in the presence of 0.4 mM ATP)1 Publication
  2. Vmax=1.5 nmol/min/mg enzyme (in the presence of 0.4 µM ATP)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401ATP2 Publications
Binding sitei45 – 451Substrate4 Publications
Binding sitei130 – 1301Substrate4 Publications
Binding sitei170 – 1701Substrate4 Publications
Binding sitei200 – 2001Substrate4 Publications
Binding sitei238 – 2381Substrate4 Publications
Binding sitei241 – 2411ATP1 Publication
Metal bindingi320 – 3201Zinc; via pros nitrogenCombined sources
Metal bindingi330 – 3301ZincCombined sources
Metal bindingi333 – 3331ZincCombined sources
Metal bindingi346 – 3461Zinc; via tele nitrogenCombined sources
Binding sitei368 – 3681Substrate4 Publications
Binding sitei407 – 4071ATP2 Publications
Binding sitei411 – 4111Substrate4 Publications
Binding sitei415 – 4151Substrate4 Publications
Binding sitei419 – 4191Substrate4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 224ATP2 Publications
Nucleotide bindingi147 – 1493ATP2 Publications
Nucleotide bindingi166 – 1683ATP2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • inositol pentakisphosphate 2-kinase activity Source: TAIR
  • inositol tetrakisphosphate 2-kinase activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular phosphate ion homeostasis Source: TAIR
  • defense response to bacterium Source: TAIR
  • defense response to fungus Source: TAIR
  • defense response to virus Source: TAIR
  • growth Source: TAIR
  • inositol phosphorylation Source: GO_Central
  • lateral root development Source: TAIR
  • myo-inositol hexakisphosphate biosynthetic process Source: TAIR
  • phosphate ion homeostasis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-ATH-1855167. Synthesis of pyrophosphates in the cytosol.
R-ATH-1855191. Synthesis of IPs in the nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol-pentakisphosphate 2-kinase (EC:2.7.1.158)
Alternative name(s):
Inositol-1,3,4,5,6-pentakisphosphate 2-kinase
Ins(1,3,4,5,6)P5 2-kinase
Short name:
AtIPK1
Short name:
InsP5 2-kinase
Gene namesi
Name:IPK1
Ordered Locus Names:At5g42810
ORF Names:MJB21.19
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G42810.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Biotechnological usei

The gene coding for this protein might be inactivated to commercially produce plants with phytate-free grain. Indeed, while the role of phytate (InsP6) accumulation in seeds is unknown, it causes nutritional and environmental problems, partly due to the inability of monogastric animals to digest it.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Inositol-pentakisphosphate 2-kinasePRO_0000110534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ93YN9.
PRIDEiQ93YN9.

Expressioni

Tissue specificityi

Strongly expressed in leaves and cauline leaves. Weakly expressed in siliques and flowers. In flower, it is expressed in the major organs of developing flower buds. Strongly expressed in sepals, petals, in the male and female organs of immature and mature flower buds. Strongly expressed in the gynoecium and carpels which are fused to form the gynoecium. Also expressed in the transmitting tissue and ovules.1 Publication

Gene expression databases

GenevisibleiQ93YN9. AT.

Interactioni

Protein-protein interaction databases

BioGridi19542. 1 interaction.
STRINGi3702.AT5G42810.1.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 126Combined sources
Beta strandi13 – 186Combined sources
Beta strandi20 – 278Combined sources
Turni32 – 365Combined sources
Beta strandi37 – 437Combined sources
Helixi49 – 513Combined sources
Helixi63 – 686Combined sources
Turni69 – 713Combined sources
Helixi73 – 764Combined sources
Helixi81 – 9111Combined sources
Helixi94 – 974Combined sources
Turni98 – 1014Combined sources
Beta strandi106 – 1105Combined sources
Helixi112 – 12514Combined sources
Helixi128 – 1303Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi163 – 1675Combined sources
Helixi177 – 1793Combined sources
Helixi182 – 1887Combined sources
Helixi192 – 20211Combined sources
Beta strandi205 – 2084Combined sources
Helixi214 – 2174Combined sources
Helixi222 – 23413Combined sources
Turni237 – 2393Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi253 – 2553Combined sources
Helixi262 – 27110Combined sources
Turni272 – 2754Combined sources
Turni280 – 2823Combined sources
Helixi283 – 29816Combined sources
Helixi300 – 3089Combined sources
Helixi315 – 32511Combined sources
Turni331 – 3355Combined sources
Helixi340 – 3478Combined sources
Helixi350 – 36819Combined sources
Beta strandi370 – 3778Combined sources
Beta strandi389 – 3924Combined sources
Turni393 – 3964Combined sources
Beta strandi397 – 40610Combined sources
Helixi415 – 43319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XALX-ray3.20A/B1-451[»]
2XAMX-ray2.20A/B1-451[»]
2XANX-ray2.20A/B1-451[»]
2XAOX-ray2.90A/B1-451[»]
2XARX-ray3.10A/B1-451[»]
3UDSX-ray3.10A/B1-451[»]
3UDTX-ray3.10A/B1-451[»]
3UDZX-ray2.50A/B1-451[»]
4AQKX-ray2.40A1-451[»]
4AXCX-ray2.25A1-451[»]
4AXDX-ray2.05A1-451[»]
4AXEX-ray2.50A1-451[»]
4AXFX-ray2.93A1-451[»]
4LV7X-ray2.60A/B1-451[»]
ProteinModelPortaliQ93YN9.
SMRiQ93YN9. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93YN9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi166 – 1705EXKPK motif

Domaini

The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.

Sequence similaritiesi

Belongs to the IPK1 type 2 family.Curated

Phylogenomic databases

eggNOGiKOG4749. Eukaryota.
ENOG410XSF2. LUCA.
HOGENOMiHOG000029746.
InParanoidiQ93YN9.
KOiK10572.
OMAiNVISQPC.
OrthoDBiEOG093609Y6.
PhylomeDBiQ93YN9.

Family and domain databases

InterProiIPR009286. Ins_P5_2-kin.
[Graphical view]
PANTHERiPTHR14456. PTHR14456. 2 hits.
PfamiPF06090. Ins_P5_2-kin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93YN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMILEEKDA SDWIYRGEGG ANLVLAYAGS SPLFVGKVIR IQKARRNDKA
60 70 80 90 100
IKNANGVVSV LTSDEQHLWR ENNELISSPN KEVLEQRYVK NVIIPLLGPK
110 120 130 140 150
HVDAGVRVSV SKEFLECVDK KVTKQRPLWR VNAANVDTSH DSALILNDHS
160 170 180 190 200
LFSQGISSGG DCISVEIKPK CGFLPTSRFI GKENMLKTSV SRFKMHQLLK
210 220 230 240 250
LEYNEISEES EYDPLDLFSG SKESVLEAIK ALYSTPQNNF RVFLNGSLIL
260 270 280 290 300
GGSGESTGRT SPEIGYAFED ALKGFIQSED GHRTECFLQL VSDAVYGSGV
310 320 330 340 350
LDRLLEIQKL DKLDIEGAIH SYYDLINQPC PICKEGKPLE AELSLHALPL
360 370 380 390 400
DESLKIVKEY LIAATAKDCS IMISFQSRNA WDSEPSGDYV SLKPTNQTFD
410 420 430 440 450
YKVHFIDLSL KPLKRMESYY KLDKKIISFY NRKQKAENTA EQIGNSKPSH

S
Length:451
Mass (Da):50,509
Last modified:December 1, 2001 - v1
Checksum:iC3172D638277D1B5
GO

Sequence cautioni

The sequence BAB10637 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ122931 mRNA. Translation: AAZ99216.1.
AB007647 Genomic DNA. Translation: BAB10637.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED94867.1.
AY059898 mRNA. Translation: AAL24380.1.
AY093362 mRNA. Translation: AAM13361.1.
RefSeqiNP_568613.1. NM_123646.3.
UniGeneiAt.8456.

Genome annotation databases

EnsemblPlantsiAT5G42810.1; AT5G42810.1; AT5G42810.
GeneIDi834292.
GrameneiAT5G42810.1; AT5G42810.1; AT5G42810.
KEGGiath:AT5G42810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ122931 mRNA. Translation: AAZ99216.1.
AB007647 Genomic DNA. Translation: BAB10637.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED94867.1.
AY059898 mRNA. Translation: AAL24380.1.
AY093362 mRNA. Translation: AAM13361.1.
RefSeqiNP_568613.1. NM_123646.3.
UniGeneiAt.8456.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XALX-ray3.20A/B1-451[»]
2XAMX-ray2.20A/B1-451[»]
2XANX-ray2.20A/B1-451[»]
2XAOX-ray2.90A/B1-451[»]
2XARX-ray3.10A/B1-451[»]
3UDSX-ray3.10A/B1-451[»]
3UDTX-ray3.10A/B1-451[»]
3UDZX-ray2.50A/B1-451[»]
4AQKX-ray2.40A1-451[»]
4AXCX-ray2.25A1-451[»]
4AXDX-ray2.05A1-451[»]
4AXEX-ray2.50A1-451[»]
4AXFX-ray2.93A1-451[»]
4LV7X-ray2.60A/B1-451[»]
ProteinModelPortaliQ93YN9.
SMRiQ93YN9. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19542. 1 interaction.
STRINGi3702.AT5G42810.1.

Proteomic databases

PaxDbiQ93YN9.
PRIDEiQ93YN9.

Protocols and materials databases

DNASUi834292.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G42810.1; AT5G42810.1; AT5G42810.
GeneIDi834292.
GrameneiAT5G42810.1; AT5G42810.1; AT5G42810.
KEGGiath:AT5G42810.

Organism-specific databases

TAIRiAT5G42810.

Phylogenomic databases

eggNOGiKOG4749. Eukaryota.
ENOG410XSF2. LUCA.
HOGENOMiHOG000029746.
InParanoidiQ93YN9.
KOiK10572.
OMAiNVISQPC.
OrthoDBiEOG093609Y6.
PhylomeDBiQ93YN9.

Enzyme and pathway databases

ReactomeiR-ATH-1855167. Synthesis of pyrophosphates in the cytosol.
R-ATH-1855191. Synthesis of IPs in the nucleus.

Miscellaneous databases

EvolutionaryTraceiQ93YN9.
PROiQ93YN9.

Gene expression databases

GenevisibleiQ93YN9. AT.

Family and domain databases

InterProiIPR009286. Ins_P5_2-kin.
[Graphical view]
PANTHERiPTHR14456. PTHR14456. 2 hits.
PfamiPF06090. Ins_P5_2-kin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIPPK_ARATH
AccessioniPrimary (citable) accession number: Q93YN9
Secondary accession number(s): Q9FMY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 1, 2001
Last modified: September 7, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.