ID   HXK3_ARATH              Reviewed;         498 AA.
AC   Q9LPS1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Hexokinase-3;
DE            EC=2.7.1.1 {ECO:0000250|UniProtKB:P93834};
DE   AltName: Full=Hexokinase-like 1;
GN   Name=HXK3 {ECO:0000305}; Synonyms=HKL1 {ECO:0000303|PubMed:19706780};
GN   OrderedLocusNames=At1g50460; ORFNames=F11F12.18;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19706780; DOI=10.1093/jxb/erp252;
RA   Karve A., Moore B.D.;
RT   "Function of Arabidopsis hexokinase-like1 as a negative regulator of plant
RT   growth.";
RL   J. Exp. Bot. 60:4137-4149(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=22366209; DOI=10.1104/pp.112.195636;
RA   Karve A., Xia X., Moore B.D.;
RT   "Arabidopsis Hexokinase-Like1 and Hexokinase1 form a critical node in
RT   mediating plant glucose and ethylene responses.";
RL   Plant Physiol. 158:1965-1975(2012).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme (By similarity).
CC       May be involved in the phosphorylation of glucose during the export
CC       from mitochondrion to cytosol (By similarity). Plays a role in plant
CC       growth and development, perhaps by mediating cross-talk between glucose
CC       and hormone response pathways (PubMed:19706780). Involved in root hair
CC       cell development by mediating certain aspects of cross talk between
CC       glucose and ethylene response pathways (PubMed:22366209).
CC       {ECO:0000250|UniProtKB:Q42525, ECO:0000269|PubMed:19706780,
CC       ECO:0000269|PubMed:22366209}.
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:0000250|UniProtKB:P93834};
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:0000250|UniProtKB:P93834};
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:0000250|UniProtKB:P93834};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000250|UniProtKB:P93834}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000250|UniProtKB:P93834}.
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   -!- TISSUE SPECIFICITY: Expressed in roots, emerging lateral roots,
CC       vascular tissues of cotyledons, roots and leaves, root and shoot
CC       meristems, anther filaments and funiculi of mature seeds.
CC       {ECO:0000269|PubMed:19706780}.
CC   -!- INDUCTION: Induced by treatment with 1-aminocyclopropanecarboxylate
CC       (ACC) and zeatin (PubMed:19706780). Repressed by treatment with
CC       abscisic acid (ABA) (PubMed:19706780). {ECO:0000269|PubMed:19706780}.
CC   -!- DISRUPTION PHENOTYPE: Dwarf plants with reduced roots and leaves growth
CC       (PubMed:19706780). Reduced sensitivity of seedlings to glucose
CC       repression of development (PubMed:19706780).
CC       {ECO:0000269|PubMed:19706780}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC012561; AAF87885.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32553.1; -; Genomic_DNA.
DR   EMBL; AY074314; AAL67011.1; -; mRNA.
DR   EMBL; AY096416; AAM20056.1; -; mRNA.
DR   PIR; A96541; A96541.
DR   RefSeq; NP_175463.1; NM_103929.4.
DR   AlphaFoldDB; Q9LPS1; -.
DR   SMR; Q9LPS1; -.
DR   BioGRID; 26693; 5.
DR   STRING; 3702.Q9LPS1; -.
DR   iPTMnet; Q9LPS1; -.
DR   PaxDb; 3702-AT1G50460-1; -.
DR   EnsemblPlants; AT1G50460.1; AT1G50460.1; AT1G50460.
DR   GeneID; 841468; -.
DR   Gramene; AT1G50460.1; AT1G50460.1; AT1G50460.
DR   KEGG; ath:AT1G50460; -.
DR   Araport; AT1G50460; -.
DR   TAIR; AT1G50460; HKL1.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_1_1; -.
DR   InParanoid; Q9LPS1; -.
DR   OMA; ADCVQQF; -.
DR   OrthoDB; 5481886at2759; -.
DR   PhylomeDB; Q9LPS1; -.
DR   BioCyc; ARA:AT1G50460-MONOMER; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:Q9LPS1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LPS1; baseline and differential.
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:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   GO; GO:0080147; P:root hair cell development; IMP:TAIR.
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; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF73; HEXOKINASE-3; 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; PS51748; HEXOKINASE_2; 1.
DR   Genevisible; Q9LPS1; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycolysis; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..498
FT                   /note="Hexokinase-3"
FT                   /id="PRO_0000259631"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..494
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          90..227
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          228..483
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         193
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
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         228
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         252
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         255
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         283
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         314
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         448
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
SQ   SEQUENCE   498 AA;  54591 MW;  1818AD18A17063D6 CRC64;
     MGKVAVAFAA VAVVAACSVA AVMVGRRMKS RRKWRTVVEI LKELEDDCDT PVGRLRQVVD
     AMAVEMHAGL ASEGGSKLKM LLTFVDDLPT GREKGTYYAL HLGGTYFRIL RVLLGDQRSY
     LDVQDVERHP IPSHLMNSTS EVLFNFLAFS LERFIEKEEN GSDSQGVRRE LAFTFSFPVK
     HTSISSGVLI KWTKGFEISE MVGQDIAECL QGALNRRGLD MHVAALVNDT VGALSLGYYH
     DPDTVVAVVF GTGSNACYLE RTDAIIKCQG LLTTSGSMVV NMEWGNFWSS HLPRTSYDID
     LDAESSNAND MGFEKMISGM YLGDIVRRVI LRMSEDSDIF GPISPVLSEP YVLRTNSVSA
     IHEDDTPELQ EVARILKDIG VSDVPLKVRK LVVKICDVVT RRAGRLAAAG IAGILKKIGR
     DGSGGITSGR SRSEIQMQKR TVVAVEGGLY MNYTMFREYM EEALVEILGE EVSQYVVVKA
     MEDGSSIGSA LLVASLQS
//