ID HXK5_ORYSJ Reviewed; 507 AA.
AC Q5W676; A0A0P0WPR6; Q0DGM7; Q94JW6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Hexokinase-5;
DE EC=2.7.1.1 {ECO:0000305|PubMed:16552590};
DE AltName: Full=Hexokinase I;
GN Name=HXK5;
GN OrderedLocusNames=Os05g0522500 {ECO:0000312|EMBL:BAF17996.1},
GN LOC_Os05g44760 {ECO:0000305};
GN ORFNames=OJ1087_C03.12, OsJ_19253 {ECO:0000312|EMBL:EEE64409.1},
GN OSJNBa0075A10.5;
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INDUCTION, 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].
RA Wu P., Jiang H.-W., Yi K.-K.;
RT "Rice hexokinase I mRNA.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-113 AND SER-186.
RX PubMed=19010999; DOI=10.1104/pp.108.131227;
RA Cho J.I., Ryoo N., Eom J.S., Lee D.W., Kim H.B., Jeong S.W., Lee Y.H.,
RA Kwon Y.K., Cho M.H., Bhoo S.H., Hahn T.R., Park Y.I., Hwang I., Sheen J.,
RA Jeon J.S.;
RT "Role of the rice hexokinases OsHXK5 and OsHXK6 as glucose sensors.";
RL Plant Physiol. 149:745-759(2009).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31671177; DOI=10.1093/jxb/erz436;
RA Lee S.K., Kim H., Cho J.I., Nguyen C.D., Moon S., Park J.E., Park H.R.,
RA Huh J.H., Jung K.H., Guiderdoni E., Jeon J.S.;
RT "Deficiency of rice hexokinase HXK5 impairs synthesis and utilization of
RT starch in pollen grains and causes male sterility.";
RL J. Exp. Bot. 71:116-125(2020).
CC -!- FUNCTION: Fructose and glucose phosphorylating enzyme
CC (PubMed:16552590). Functions as a glucose sensor for plant growth and
CC photosynthesis (PubMed:19010999). Is essential for pollen development,
CC germination, and tube growth (PubMed:31671177). Its activity is
CC necessary for the starch utilization pathway during pollen germination
CC and tube growth, as well as for starch biosynthesis during pollen
CC maturation (PubMed:31671177). {ECO:0000269|PubMed:16552590,
CC ECO:0000269|PubMed:19010999, ECO:0000269|PubMed:31671177}.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, immature
CC seeds, endosperm and seed coat. {ECO:0000269|PubMed:16552590}.
CC -!- DEVELOPMENTAL STAGE: Expressed during flower development until 15 days
CC after flowering (PubMed:16552590). In pollen development, expression
CC increases gradually from meiosis/tetrad stage to mature pollen stage,
CC with the highest expression in the latter (PubMed:31671177).
CC {ECO:0000269|PubMed:16552590, ECO:0000269|PubMed:31671177}.
CC -!- INDUCTION: By glucose or fructose treatment in leaves.
CC {ECO:0000269|PubMed:16552590}.
CC -!- DISRUPTION PHENOTYPE: Male sterility of pollen grains due to impaired
CC synthesis and utilization of starch in pollen grains.
CC {ECO:0000269|PubMed:31671177}.
CC -!- MISCELLANEOUS: Plants over-expressing HXK5 exhibit hypersensitive plant
CC growth retardation and enhanced repression of the photosynthetic gene
CC RbcS in response to glucose treatment. {ECO:0000269|PubMed:19010999}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; DQ116387; AAZ93622.1; -; mRNA.
DR EMBL; AF372831; AAK51559.1; -; mRNA.
DR EMBL; AC118284; AAV59322.1; -; Genomic_DNA.
DR EMBL; AC144740; AAV44032.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17996.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94954.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64409.1; -; Genomic_DNA.
DR RefSeq; XP_015639323.1; XM_015783837.1.
DR AlphaFoldDB; Q5W676; -.
DR SMR; Q5W676; -.
DR STRING; 39947.Q5W676; -.
DR PaxDb; 39947-Q5W676; -.
DR EnsemblPlants; Os05t0522500-01; Os05t0522500-01; Os05g0522500.
DR GeneID; 4339361; -.
DR Gramene; Os05t0522500-01; Os05t0522500-01; Os05g0522500.
DR KEGG; osa:4339361; -.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_5_1_1; -.
DR InParanoid; Q5W676; -.
DR OMA; HWDKGWD; -.
DR OrthoDB; 5481886at2759; -.
DR BRENDA; 2.7.1.1; 4460.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q5W676; OS.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
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; IMP:CACAO.
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 GO; GO:0009749; P:response to glucose; IMP:CACAO.
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:SF22; HEXOKINASE-5; 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 ATP-binding; Chloroplast; Glycolysis; Kinase; Membrane; Nucleotide-binding;
KW Plastid; Plastid outer membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Hexokinase-5"
FT /id="PRO_0000247568"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..498
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 99..237
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 238..487
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 113
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 114
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 115
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 203
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 204
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 238
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 239
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 262
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 265
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 293
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 324
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 452
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT MUTAGEN 113
FT /note="G->D: Abolishes glucose phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:19010999"
FT MUTAGEN 186
FT /note="S->A: Abolishes glucose phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:19010999"
SQ SEQUENCE 507 AA; 54659 MW; 9A3A685AF1E28D7A CRC64;
MGKAAAVGTA VVVAAAVGVA VVLARRRRRR DLELVEGAAA ERKRKVAAVI EDVEHALSTP
TALLRGISDA MVTEMERGLR GDSHAMVKML ITYVDNLPTG NEQGLFYALD LGGTNFRVLR
VQLGGKEKRV VQQQYEEVSI PPHLMVGTSM ELFDFIASAL SKFVDTEGDD FHLPEGRQRE
LGFTFSFPVS QTSISSGTLI KWTKGFSIND AVGEDVVSEL GKAMERQGLD MKIAALVNDT
VGTLAGGRYA DNSVVAAIIL GTGTNAAYVE NANAIPKWTG LLPRSGNMVI NTEWGSFKSD
KLPLSEFDKA MDFESLNPGE QIYEKLISGM YLGEIVRRIL LKLAHDAALF GDVVPSKLEQ
PFVLRTPDMS AMHHDSSHDL KTVGAKLKDI VGVPDTSLEV RYITSHICDI VAERAARLAA
AGIYGVLKKL GRDKMPKDGS KMPRTVIALD GGLYEHYKKF SSCLESTLTD LLGDDVSSSV
VTKLANDGSG IGAALLAASH SQYAEID
//
