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P93834 (HXK2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexokinase-2

EC=2.7.1.1
Gene names
Name:HXK2
Ordered Locus Names:At2g19860
ORF Names:F6F22.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Fructose and glucose phosphorylating enzyme. May be involved in the phosphorylation of glucose during the export from mitochondrion to cytosol. Acts as sugar sensor which may regulate sugar-dependent gene repression or activation. Mediates the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. May regulate the execution of program cell death in plant cells. Ref.1 Ref.8

Catalytic activity

ATP + D-hexose = ADP + D-hexose 6-phosphate.

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein Ref.6 Ref.7.

Tissue specificity

Highly expressed in siliques, at intermediate levels in roots and flowers, and at lower levels in stems, rosette and cauline leaves. Ref.1

Disruption phenotype

Plants are overall smaller with a reduced number of flowers and siliques and display a glucose-insensitive phenotype which allows them to grow on high glucose concentration medium (>6% glucose). Ref.1

Sequence similarities

Belongs to the hexokinase family.

Contains 1 hexokinase type-1 domain.

Contains 1 hexokinase type-2 domain.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate phosphorylation

Inferred from direct assay PubMed 18481082. Source: GOC

glucose 6-phosphate metabolic process

Inferred from direct assay PubMed 11851922. Source: GOC

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hexokinase-dependent signaling

Inferred from mutant phenotype Ref.1. Source: TAIR

programmed cell death

Inferred from mutant phenotype Ref.8. Source: TAIR

sugar mediated signaling pathway

Inferred from mutant phenotype Ref.1. Source: TAIR

   Cellular_componentintegral component of mitochondrial outer membrane

Inferred from direct assay PubMed 21896887. Source: TAIR

mitochondrion

Inferred from direct assay Ref.6Ref.7PubMed 16618929PubMed 18481082PubMed 22923678. Source: TAIR

plastid

Inferred from direct assay PubMed 16618929. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fructokinase activity

Inferred from direct assay PubMed 18481082. Source: TAIR

glucokinase activity

Inferred from direct assay PubMed 11851922. Source: TAIR

hexokinase activity

Inferred from mutant phenotype Ref.1. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P93834-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Hexokinase-2
PRO_0000197613

Regions

Transmembrane4 – 2421Helical; Potential
Domain40 – 241202Hexokinase type-1
Domain246 – 488243Hexokinase type-2
Nucleotide binding101 – 1066ATP Potential
Region171 – 19727Glucose-binding Potential

Experimental info

Sequence conflict2421N → S in AAO24584. Ref.4
Sequence conflict2421N → S in BAE99655. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: FEAF0B860D7531C9

FASTA50254,490
        10         20         30         40         50         60 
MGKVAVATTV VCSVAVCAAA ALIVRRRMKS AGKWARVIEI LKAFEEDCAT PIAKLRQVAD 

        70         80         90        100        110        120 
AMTVEMHAGL ASEGGSKLKM LISYVDNLPS GDETGFFYAL DLGGTNFRVM RVLLGGKHDR 

       130        140        150        160        170        180 
VVKREFKEES IPPHLMTGKS HELFDFIVDV LAKFVATEGE DFHLPPGRQR ELGFTFSFPV 

       190        200        210        220        230        240 
KQLSLSSGTL INWTKGFSID DTVDKDVVGE LVKAMERVGL DMLVAALVND TIGTLAGGRY 

       250        260        270        280        290        300 
TNPDVVVAVI LGTGTNAAYV ERAHAIPKWH GLLPKSGEMV INMEWGNFRS SHLPLTEYDH 

       310        320        330        340        350        360 
SLDVDSLNPG EQILEKIISG MYLGEILRRV LLKMAEEAAF FGDIVPPKLK IPFIIRTPNM 

       370        380        390        400        410        420 
SAMHSDTSPD LKVVGSKLKD ILEVQTSSLK MRKVVISLCN IIASRGARLS AAGIYGILKK 

       430        440        450        460        470        480 
IGRDATKDGE AQKSVIAMDG GLFEHYTQFS ESMKSSLKEL LGDEVSESVE VILSNDGSGV 

       490        500 
GAALLAASHS QYLELEDDSE TS 

« Hide

References

« Hide 'large scale' references
[1]"Hexokinase as a sugar sensor in higher plants."
Jang J.-C., Leon P., Zhou L., Sheen J.
Plant Cell 9:5-19(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Strain: cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells."
Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R., Leaver C.J., Sweetlove L.J.
Plant Cell 15:2140-2151(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
Strain: cv. Landsberg erecta.
[8]"Mitochondria-associated hexokinases play a role in the control of programmed cell death in Nicotiana benthamiana."
Kim M., Lim J.-H., Ahn C.S., Park K., Kim G.T., Kim W.T., Pai H.-S.
Plant Cell 18:2341-2355(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28215 mRNA. Translation: AAB49911.1.
AC005169 Genomic DNA. Translation: AAC62130.1.
CP002685 Genomic DNA. Translation: AEC06934.1.
BT003152 mRNA. Translation: AAO24584.1.
AK227668 mRNA. Translation: BAE99655.1.
PIRA84582.
RefSeqNP_179576.1. NM_127544.2.
UniGeneAt.12899.

3D structure databases

ProteinModelPortalP93834.
SMRP93834. Positions 55-487.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP93834.
PRIDEP93834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G19860.1; AT2G19860.1; AT2G19860. [P93834-1]
GeneID816505.
KEGGath:AT2G19860.

Organism-specific databases

GeneFarm4269. 430.
TAIRAT2G19860.

Phylogenomic databases

eggNOGCOG5026.
HOGENOMHOG000162670.
InParanoidP93834.
KOK00844.
OMAGFNCAGV.
PhylomeDBP93834.
ProtClustDBPLN02405.

Enzyme and pathway databases

BioCycARA:GQT-1724-MONOMER.
MetaCyc:AT2G19860-MONOMER.

Gene expression databases

ArrayExpressP93834.
GenevestigatorP93834.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERPTHR19443. PTHR19443. 1 hit.
PfamPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHXK2_ARATH
AccessionPrimary (citable) accession number: P93834
Secondary accession number(s): Q0WT93, Q84WJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names