ID   HXK1_ORYSJ              Reviewed;         498 AA.
AC   Q8LH82; Q0D6S1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Hexokinase-1;
DE            EC=2.7.1.1 {ECO:0000305|PubMed:16552590};
GN   Name=HXK1; OrderedLocusNames=Os07g0446800, LOC_Os07g26540;
GN   ORFNames=P0030H06.133, P0475E07.113;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND NOMENCLATURE.
RC   STRAIN=cv. Jinmi;
RX   PubMed=16552590; DOI=10.1007/s00425-006-0251-y;
RA   Cho J.-I., Ryoo N., Ko S., Lee S.-K., Lee J., Jung K.-H., Lee Y.-H.,
RA   Bhoo S.H., Winderickx J., An G., Hahn T.-R., Jeon J.-S.;
RT   "Structure, expression, and functional analysis of the hexokinase gene
RT   family in rice (Oryza sativa L.).";
RL   Planta 224:598-611(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Zhonghua 15; TISSUE=Flower;
RA   Wang Y.D., Cheng W., Wang X.S., Zhou X.J.;
RT   "The hexokinase gene family in rice.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=34879830; DOI=10.1186/s12870-021-03343-5;
RA   Zheng S., Lu J., Yu D., Li J., Zhou H., Jiang D., Liu Z., Zhuang C.;
RT   "Hexokinase gene OsHXK1 positively regulates leaf senescence in rice.";
RL   BMC Plant Biol. 21:580-580(2021).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme
CC       (PubMed:16552590). Acts as a positive regulator of leaf senescence by
CC       mediating glucose accumulation and inducing an increase in reactive
CC       oxygen species (ROS) (PubMed:34879830). {ECO:0000269|PubMed:16552590,
CC       ECO:0000269|PubMed:34879830}.
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:16552590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000305|PubMed:16552590};
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:16552590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000305|PubMed:16552590};
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:16552590};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000305|PubMed:16552590};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000305|PubMed:16552590}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000305|PubMed:16552590}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in senescent leaves.
CC       {ECO:0000269|PubMed:34879830}.
CC   -!- MISCELLANEOUS: Plants over-expressing HXK1 exhibit early leaf
CC       senescence phenotype. {ECO:0000269|PubMed:34879830}.
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; DQ116383; AAZ93618.1; -; mRNA.
DR   EMBL; AY884164; AAX68417.1; -; mRNA.
DR   EMBL; AP004395; BAC10209.1; -; Genomic_DNA.
DR   EMBL; AP004668; BAC16101.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF21452.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT01294.1; -; Genomic_DNA.
DR   RefSeq; XP_015645221.1; XM_015789735.1.
DR   AlphaFoldDB; Q8LH82; -.
DR   SMR; Q8LH82; -.
DR   STRING; 39947.Q8LH82; -.
DR   PaxDb; 39947-Q8LH82; -.
DR   EnsemblPlants; Os07t0446800-01; Os07t0446800-01; Os07g0446800.
DR   GeneID; 4343113; -.
DR   Gramene; Os07t0446800-01; Os07t0446800-01; Os07g0446800.
DR   KEGG; osa:4343113; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_1_1; -.
DR   InParanoid; Q8LH82; -.
DR   OMA; TEWGSFA; -.
DR   OrthoDB; 1343030at2759; -.
DR   BRENDA; 2.7.1.1; 4460.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; 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:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
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; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF82; HEXOKINASE-1; 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; Q8LH82; OS.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..498
FT                   /note="Hexokinase-1"
FT                   /id="PRO_0000247564"
FT   DOMAIN          39..492
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          95..233
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          234..481
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         109
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         110
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         111
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         199
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         200
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         234
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         235
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         258
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         261
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         290
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         321
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         446
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
SQ   SEQUENCE   498 AA;  51772 MW;  6DC7BD48B62C985E CRC64;
     MAAAAVAADQ KVVTMTSLRE GCACAAPPAA AAPPMPKMAA AQRVVAELRE ACATPAARLA
     EVAAAMAGEM EAGLAVEGGS SEMKMIVSYV DSLPTGGEEG SYYALDLGGT NFRVLRVRLA
     GGGVAERVAR EVPIPPGLMS GGGATSECLF GFIASALAEF VGEEEEEGGL DGGERELGFT
     FSFPVHQTSI ASGTLIRWTK AFAVDDAIGE DVVAALQAAM SERGLDMRVS ALINDTVGTL
     AAGSYYDEDV VAAVILGTGT NAAYVEDATA IAKLHPSQLP ASNTMVINTE WGSFASPCLP
     LTEFDEALDQ ESLNPGEQTY EKLISGMYLG EIVRRVLLKI SSRCPSLLGG AGELATPFVL
     RTPDVSAMHH DETPDLSIVG EKLERTLGIR GTSPEARRMV VEVCDIVATR AARLAAAGIV
     GILKKIGRVD GGEGRRRRSV VAVDGGLFEH YGKFRRCMES AVRELLGEAA AERVVVKLAS
     DGSGLGAALV AAAHSQRA
//