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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)DescriptionActionsGraphical viewLength
Binding sitei40ATP2 Publications1
Binding sitei45Substrate4 Publications1
Binding sitei130Substrate4 Publications1
Binding sitei170Substrate4 Publications1
Binding sitei200Substrate4 Publications1
Binding sitei238Substrate4 Publications1
Binding sitei241ATP1 Publication1
Metal bindingi320Zinc; via pros nitrogenCombined sources1
Metal bindingi330ZincCombined sources1
Metal bindingi333ZincCombined sources1
Metal bindingi346Zinc; via tele nitrogenCombined sources1
Binding sitei368Substrate4 Publications1
Binding sitei407ATP2 Publications1
Binding sitei411Substrate4 Publications1
Binding sitei415Substrate4 Publications1
Binding sitei419Substrate4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 22ATP2 Publications4
Nucleotide bindingi147 – 149ATP2 Publications3
Nucleotide bindingi166 – 168ATP2 Publications3

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001105341 – 451Inositol-pentakisphosphate 2-kinaseAdd BLAST451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ93YN9.

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 interactor.
STRINGi3702.AT5G42810.1.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 12Combined sources6
Beta strandi13 – 18Combined sources6
Beta strandi20 – 27Combined sources8
Turni32 – 36Combined sources5
Beta strandi37 – 43Combined sources7
Helixi49 – 51Combined sources3
Helixi63 – 68Combined sources6
Turni69 – 71Combined sources3
Helixi73 – 76Combined sources4
Helixi81 – 91Combined sources11
Helixi94 – 97Combined sources4
Turni98 – 101Combined sources4
Beta strandi106 – 110Combined sources5
Helixi112 – 125Combined sources14
Helixi128 – 130Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi142 – 147Combined sources6
Beta strandi152 – 155Combined sources4
Beta strandi163 – 167Combined sources5
Helixi177 – 179Combined sources3
Helixi182 – 188Combined sources7
Helixi192 – 202Combined sources11
Beta strandi205 – 208Combined sources4
Helixi214 – 217Combined sources4
Helixi222 – 234Combined sources13
Turni237 – 239Combined sources3
Beta strandi240 – 244Combined sources5
Beta strandi247 – 250Combined sources4
Beta strandi253 – 255Combined sources3
Helixi262 – 271Combined sources10
Turni272 – 275Combined sources4
Turni280 – 282Combined sources3
Helixi283 – 298Combined sources16
Helixi300 – 308Combined sources9
Helixi315 – 325Combined sources11
Turni331 – 335Combined sources5
Helixi340 – 347Combined sources8
Helixi350 – 368Combined sources19
Beta strandi370 – 377Combined sources8
Beta strandi389 – 392Combined sources4
Turni393 – 396Combined sources4
Beta strandi397 – 406Combined sources10
Helixi415 – 433Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93YN9.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi166 – 170EXKPK motif5

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_123646.4.
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_123646.4.
UniGeneiAt.8456.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19542. 1 interactor.
STRINGi3702.AT5G42810.1.

Proteomic databases

PaxDbiQ93YN9.

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: November 30, 2016
This is version 98 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.