ID HXK7_ORYSJ Reviewed; 463 AA.
AC Q1WM16; Q2KNB6; Q75KY7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=Hexokinase-7;
DE EC=2.7.1.1 {ECO:0000305|PubMed:16552590};
DE AltName: Full=Hexokinase-6;
GN Name=HXK7; Synonyms=HXK6; OrderedLocusNames=Os05g0187100, LOC_Os05g09500;
GN ORFNames=OJ1097_A12.3;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL 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].
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=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=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 MUTAGENESIS OF GLY-76 AND SER-148.
RX PubMed=25951042; DOI=10.1111/jipb.12366;
RA Kim H.B., Cho J.I., Ryoo N., Shin D.H., Park Y.I., Hwang Y.S., Lee S.K.,
RA An G., Jeon J.S.;
RT "Role of rice cytosolic hexokinase OsHXK7 in sugar signaling and
RT metabolism.";
RL J. Integr. Plant Biol. 58:127-135(2016).
CC -!- FUNCTION: Fructose and glucose phosphorylating enzyme
CC (PubMed:16552590). Functions in sugar signaling via a glycolysis-
CC dependent manner under aerobic conditions, but its signaling role is
CC suppressed when oxygen is deficient (PubMed:25951042).
CC {ECO:0000269|PubMed:16552590, ECO:0000269|PubMed:25951042}.
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: Cytoplasm {ECO:0000305|PubMed:16552590}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, immature seeds
CC and seed coat. {ECO:0000269|PubMed:16552590}.
CC -!- DEVELOPMENTAL STAGE: Expressed during flower development until 15 days
CC after flowering. {ECO:0000269|PubMed:16552590}.
CC -!- INDUCTION: Down-regulated by glucose or fructose treatment in leaves
CC and immature seeds. {ECO:0000269|PubMed:16552590}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS86398.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ116389; AAZ93624.1; -; mRNA.
DR EMBL; AY884169; AAX68422.1; -; mRNA.
DR EMBL; AC093954; AAS86398.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015637554.1; XM_015782068.1.
DR AlphaFoldDB; Q1WM16; -.
DR SMR; Q1WM16; -.
DR STRING; 39947.Q1WM16; -.
DR PaxDb; 39947-Q1WM16; -.
DR EnsemblPlants; Os05t0187100-02; Os05t0187100-02; Os05g0187100.
DR GeneID; 4338010; -.
DR Gramene; Os05t0187100-02; Os05t0187100-02; Os05g0187100.
DR KEGG; osa:4338010; -.
DR eggNOG; KOG1369; Eukaryota.
DR InParanoid; Q1WM16; -.
DR OrthoDB; 5481886at2759; -.
DR BRENDA; 2.7.1.1; 4460.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q1WM16; baseline and differential.
DR Genevisible; Q1WM16; OS.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..463
FT /note="Hexokinase-7"
FT /id="PRO_0000247570"
FT DOMAIN 7..456
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 62..199
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 200..445
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 76
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 77
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 78
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 165
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 166
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 201
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 224
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 227
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
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 286
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT BINDING 410
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT MUTAGEN 76
FT /note="G->D: Abolishes glucose phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:25951042"
FT MUTAGEN 148
FT /note="S->A: Abolishes glucose phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:25951042"
FT CONFLICT 199
FT /note="I -> T (in Ref. 1; AAZ93624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 49761 MW; C6E3D7D1BB2E19B5 CRC64;
MVAAAVAAAE QVVAALREEC ATPAARLDGV AAAMAGEMAA GLAEEGGSKI KMIVSYVDNL
PNGTEEGLFY ALDLGGTNFR VLRVQLAGKE KRVVKRESRE VSIPPHLMSG NSSELFGFIA
SALAKFVADE GHNAVFNDRQ RELGFTFSFP VRQTSIASGT LIKWTKAFSI DDAVGEDVVA
ELQMAMEKQG LDMRVSALIN DTVGTLAAGS YYDEDIVVGV ILGTGSNAAY LEKANAIPKL
EGELPKSGNM VINTEWGNFS SSCLPITEYD EALDKESLNP GEQIFEKLIS GMYLGEIVRR
VLLKISLQSS IFGNLDQTKL KTRFILRTPD ISVMHHDGTP DLRIVAEKLA DNLKITDTSL
ETRKMVVEIC DIVTRRSARL AAAGIVGILR KIGRGVPGDK RKSVIAIDGG LYEHYTEFRQ
CLETTLTELL GEEASKSVAV KLANDGSGLG AALIAAAHSQ YLN
//
