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 03-AUG-2022, entry version 161.
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=10.2307/3870367;
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 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.AT2G19860.1; -.
DR PaxDb; P93834; -.
DR PRIDE; P93834; -.
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; locus:2051920; AT2G19860.
DR eggNOG; KOG1369; Eukaryota.
DR InParanoid; P93834; -.
DR OMA; FVEKHDM; -.
DR PhylomeDB; P93834; -.
DR BioCyc; ARA:AT2G19860-MON; -.
DR BioCyc; MetaCyc:AT2G19860-MON; -.
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:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:TAIR.
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:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0009747; P:hexokinase-dependent signaling; IMP:TAIR.
DR GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
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; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 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 171..197
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 229..476
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 101..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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
