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Database: UniProt/SWISS-PROT
Entry: HXK2_ARATH
LinkDB: HXK2_ARATH
Original site: HXK2_ARATH 
ID   HXK2_ARATH              Reviewed;         502 AA.
AC   P93834; Q0WT93; Q84WJ5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Hexokinase-2;
DE            EC=2.7.1.1 {ECO:0000305|PubMed:9014361};
GN   Name=HXK2; OrderedLocusNames=At2g19860; ORFNames=F6F22.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9014361; DOI=10.1105/tpc.9.1.5;
RA   Jang J.-C., Leon P., Zhou L., Sheen J.;
RT   "Hexokinase as a sugar sensor in higher plants.";
RL   Plant Cell 9:5-19(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=12953116; DOI=10.1105/tpc.012500;
RA   Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R.,
RA   Leaver C.J., Sweetlove L.J.;
RT   "Enzymes of glycolysis are functionally associated with the mitochondrion
RT   in Arabidopsis cells.";
RL   Plant Cell 15:2140-2151(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=16920781; DOI=10.1105/tpc.106.041509;
RA   Kim M., Lim J.-H., Ahn C.S., Park K., Kim G.T., Kim W.T., Pai H.-S.;
RT   "Mitochondria-associated hexokinases play a role in the control of
RT   programmed cell death in Nicotiana benthamiana.";
RL   Plant Cell 18:2341-2355(2006).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme (PubMed:9014361).
CC       May be involved in the phosphorylation of glucose during the export
CC       from mitochondrion to cytosol (PubMed:9014361). Acts as a sugar sensor
CC       which may regulate sugar-dependent gene repression or activation
CC       (PubMed:9014361). Mediates the effects of sugar on plant growth and
CC       development independently of its catalytic activity or the sugar
CC       metabolism (PubMed:9014361). May regulate the execution of program cell
CC       death in plant cells (PubMed:16920781). {ECO:0000269|PubMed:16920781,
CC       ECO:0000269|PubMed:9014361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000305|PubMed:9014361};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000305|PubMed:9014361};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000305|PubMed:9014361};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000305|PubMed:9014361}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000305|PubMed:9014361}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:12953116, ECO:0000269|PubMed:14671022}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:12953116,
CC       ECO:0000269|PubMed:14671022}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P93834-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Highly expressed in siliques, at intermediate
CC       levels in roots and flowers, and at lower levels in stems, rosette and
CC       cauline leaves. {ECO:0000269|PubMed:9014361}.
CC   -!- DISRUPTION PHENOTYPE: Plants are overall smaller with a reduced number
CC       of flowers and siliques and display a glucose-insensitive phenotype
CC       which allows them to grow on high glucose concentration medium (>6%
CC       glucose). {ECO:0000269|PubMed:9014361}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; U28215; AAB49911.1; -; mRNA.
DR   EMBL; AC005169; AAC62130.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06934.1; -; Genomic_DNA.
DR   EMBL; BT003152; AAO24584.1; -; mRNA.
DR   EMBL; AK227668; BAE99655.1; -; mRNA.
DR   PIR; A84582; A84582.
DR   RefSeq; NP_179576.1; NM_127544.3. [P93834-1]
DR   AlphaFoldDB; P93834; -.
DR   SMR; P93834; -.
DR   STRING; 3702.P93834; -.
DR   PaxDb; 3702-AT2G19860-1; -.
DR   ProteomicsDB; 228878; -. [P93834-1]
DR   EnsemblPlants; AT2G19860.1; AT2G19860.1; AT2G19860. [P93834-1]
DR   GeneID; 816505; -.
DR   Gramene; AT2G19860.1; AT2G19860.1; AT2G19860. [P93834-1]
DR   KEGG; ath:AT2G19860; -.
DR   Araport; AT2G19860; -.
DR   TAIR; AT2G19860; HXK2.
DR   eggNOG; KOG1369; Eukaryota.
DR   InParanoid; P93834; -.
DR   OMA; YHPNCRI; -.
DR   OrthoDB; 5481886at2759; -.
DR   PhylomeDB; P93834; -.
DR   BioCyc; ARA:AT2G19860-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G19860-MONOMER; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:P93834; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93834; baseline and differential.
DR   Genevisible; P93834; AT.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IDA:TAIR.
DR   GO; GO:0004340; F:glucokinase activity; IDA:TAIR.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IMP:TAIR.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009747; P:hexokinase-dependent signaling; IMP:TAIR.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR   GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF79; HEXOKINASE-2; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Glycolysis; Kinase; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Hexokinase-2"
FT                   /id="PRO_0000197613"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..487
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          90..228
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          229..476
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         104
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         105
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         106
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         194
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         195
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         229
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         230
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         253
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         256
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         284
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         315
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         441
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   CONFLICT        242
FT                   /note="N -> S (in Ref. 4; AAO24584 and 5; BAE99655)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  54490 MW;  FEAF0B860D7531C9 CRC64;
     MGKVAVATTV VCSVAVCAAA ALIVRRRMKS AGKWARVIEI LKAFEEDCAT PIAKLRQVAD
     AMTVEMHAGL ASEGGSKLKM LISYVDNLPS GDETGFFYAL DLGGTNFRVM RVLLGGKHDR
     VVKREFKEES IPPHLMTGKS HELFDFIVDV LAKFVATEGE DFHLPPGRQR ELGFTFSFPV
     KQLSLSSGTL INWTKGFSID DTVDKDVVGE LVKAMERVGL DMLVAALVND TIGTLAGGRY
     TNPDVVVAVI LGTGTNAAYV ERAHAIPKWH GLLPKSGEMV INMEWGNFRS SHLPLTEYDH
     SLDVDSLNPG EQILEKIISG MYLGEILRRV LLKMAEEAAF FGDIVPPKLK IPFIIRTPNM
     SAMHSDTSPD LKVVGSKLKD ILEVQTSSLK MRKVVISLCN IIASRGARLS AAGIYGILKK
     IGRDATKDGE AQKSVIAMDG GLFEHYTQFS ESMKSSLKEL LGDEVSESVE VILSNDGSGV
     GAALLAASHS QYLELEDDSE TS
//
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