ID   HXK3_ORYSJ              Reviewed;         500 AA.
AC   Q2KNB4; Q5JLP7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Hexokinase-3 {ECO:0000303|PubMed:16552590};
DE            EC=2.7.1.1 {ECO:0000305|PubMed:16552590};
DE   AltName: Full=Hexokinase-8;
DE   AltName: Full=Protein SHORT AND NARROW GRAIN 1 {ECO:0000303|PubMed:35941236};
GN   Name=HXK3 {ECO:0000303|PubMed:16552590};
GN   Synonyms=HXK8, SNG1 {ECO:0000303|PubMed:35941236};
GN   OrderedLocusNames=Os01g0940100, LOC_Os01g71320;
GN   ORFNames=B1150F11.26-1;
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].
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=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=35941236; DOI=10.1007/s00122-022-04189-7;
RA   Yun P., Li Y., Wu B., Zhu Y., Wang K., Li P., Gao G., Zhang Q., Li X.,
RA   Li Z., He Y.;
RT   "OsHXK3 encodes a hexokinase-like protein that positively regulates grain
RT   size in rice.";
RL   Theor. Appl. Genet. 135:3417-3431(2022).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme
CC       (PubMed:16552590). Involved in the regulation of cell expansion in
CC       spikelet hulls, grain size, and gibberellin biosynthesis and
CC       homeostasis (PubMed:35941236). {ECO:0000269|PubMed:16552590,
CC       ECO:0000269|PubMed:35941236}.
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: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:35941236}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, immature seeds
CC       and seed coat (PubMed:16552590). Expressed in young shoots, tiller
CC       buds, endosperm seven days after fertilization, and interconnecting
CC       tissues such as pulvini and nodes (PubMed:35941236).
CC       {ECO:0000269|PubMed:16552590, ECO:0000269|PubMed:35941236}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during flower development until 8 days
CC       after flowering. {ECO:0000269|PubMed:16552590}.
CC   -!- INDUCTION: Not induced by glucose or fructose treatment in leaves.
CC       {ECO:0000269|PubMed:16552590}.
CC   -!- DISRUPTION PHENOTYPE: Decreased grain length, grain width, and grain
CC       filling (PubMed:35941236). Delayed seed germination and retarded
CC       seedling growth (PubMed:35941236). {ECO:0000269|PubMed:35941236}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD87613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ116385; AAZ93620.1; -; mRNA.
DR   EMBL; AY884171; AAX68424.1; -; mRNA.
DR   EMBL; AP003412; BAD87613.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015621344.1; XM_015765858.1.
DR   AlphaFoldDB; Q2KNB4; -.
DR   SMR; Q2KNB4; -.
DR   STRING; 39947.Q2KNB4; -.
DR   PaxDb; 39947-Q2KNB4; -.
DR   EnsemblPlants; Os01t0940100-01; Os01t0940100-01; Os01g0940100.
DR   GeneID; 4326516; -.
DR   Gramene; Os01t0940100-01; Os01t0940100-01; Os01g0940100.
DR   KEGG; osa:4326516; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   InParanoid; Q2KNB4; -.
DR   OrthoDB; 5481886at2759; -.
DR   BRENDA; 2.7.1.1; 4460.
DR   PlantReactome; R-OSA-1119570; Cytosolic glycolysis.
DR   PlantReactome; R-OSA-1119595; Mannose degradation.
DR   PlantReactome; R-OSA-1119601; Trehalose degradation II.
DR   PlantReactome; R-OSA-1119628; GDP-mannose metabolism.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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; IEA:RHEA.
DR   GO; GO:0004340; F:glucokinase activity; IEA:RHEA.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
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   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:SF6; HEXOKINASE-4; 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.
DR   Genevisible; Q2KNB4; OS.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycolysis; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="Hexokinase-3"
FT                   /id="PRO_0000247566"
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..222
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          223..476
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         106
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         188
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         189
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         223
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         224
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         247
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         250
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         278
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         309
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         441
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
SQ   SEQUENCE   500 AA;  53794 MW;  0179231A6AC47A2C CRC64;
     MGRVGLGVAV GCAAVTCAIA AALVARRASA RARWRRAVAL LREFEEGCAT PPARLRQVVD
     AMVVEMHAGL ASDGGSKLKM LLTFVDALPS GSEEGVYYSI DLGGTNFRVL RVQVGAGSVI
     VNQKVEQQPI PEELTKGTTE GLFNFVALAL KNFLEGEDDQ DGKMALGFTF SFPVRQISVS
     SGSLIRWTKG FSIRDTVGRD VAQCLNEALA NCGLNVRVTA LVNDTVGTLA LGHYYDEDTV
     AAVIIGSGTN ACYIERTDAI IKCQGLLTNS GGMVVNMEWG NFWSSHLPRT PYDILLDDET
     HNRNDQGFEK MISGMYLGEI ARLVFHRMAQ ESDVFGDAAD SLSNPFILST PFLAAIREDD
     SPDLSEVRRI LREHLKIPDA PLKTRRLVVK VCDIVTRRAA RLAAAGIVGI LKKLGRDGSG
     AASSGRGRGQ PRRTVVAIEG GLYQGYPVFR EYLDEALVEI LGEEVARNVT LRVTEDGSGV
     GAALLAAVHS SNRQQQGGPI
//