ID HXK2_ORYSJ Reviewed; 494 AA. AC Q2KNB9; Q6I5H8; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 24-JAN-2024, entry version 88. DE RecName: Full=Hexokinase-2; DE EC=2.7.1.1 {ECO:0000305|PubMed:16552590}; DE AltName: Full=Hexokinase-3; GN Name=HXK2; Synonyms=HXK3; GN OrderedLocusNames=Os05g0532600, LOC_Os05g45590; GN ORFNames=OSJNBa0053E05.8; 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=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). CC -!- FUNCTION: Fructose and glucose phosphorylating enzyme. CC {ECO:0000269|PubMed:16552590}. 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: 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. {ECO:0000269|PubMed:16552590}. CC -!- INDUCTION: By glucose or fructose treatment in leaves. CC {ECO:0000269|PubMed:16552590}. CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE- CC ProRule:PRU01084, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAT47078.1; Type=Erroneous gene model prediction; Evidence={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; DQ116384; AAZ93619.1; -; mRNA. DR EMBL; AY884166; AAX68419.1; -; mRNA. DR EMBL; AC121365; AAT47078.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015637797.1; XM_015782311.1. DR AlphaFoldDB; Q2KNB9; -. DR SMR; Q2KNB9; -. DR STRING; 39947.Q2KNB9; -. DR PaxDb; 39947-Q2KNB9; -. DR EnsemblPlants; Os05t0532600-01; Os05t0532600-01; Os05g0532600. DR GeneID; 4339420; -. DR Gramene; Os05t0532600-01; Os05t0532600-01; Os05g0532600. DR KEGG; osa:4339420; -. DR eggNOG; KOG1369; Eukaryota. DR InParanoid; Q2KNB9; -. 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 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:SF16; HEXOKINASE TYPE 1-RELATED; 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 2: Evidence at transcript level; KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..494 FT /note="Hexokinase-2" FT /id="PRO_0000247565" FT DOMAIN 32..483 FT /note="Hexokinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 87..225 FT /note="Hexokinase small subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 226..472 FT /note="Hexokinase large subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT BINDING 101 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 102 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 103 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 191 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 192 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 226 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" 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 250 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 253 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 281 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 312 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" FT BINDING 437 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q8LQ68" SQ SEQUENCE 494 AA; 53626 MW; CBD4744352238E0D CRC64; MRKAAAAAVA AAAAVGVALL VRRQLREAKR WGRADAVLRE LEERCAAPPG RLRQVADAMA VEMHAGLASE GGSKLKMIIS YVDALPSGEE KGVFYALDLG GTNFRVLRVQ LGGKEGRVIK QEHDEISIPP HLMTGGSNEL FDFIASSLAK FVASEGEDFH LAEGRQRELG FTFSFPVKQT SIASGTLINW TKGFSIDETV GEDVVTELTK ALERQGLDMK VTALINDTIG TLAGGRYDDN DVIAAVILGT GTNAAYVERA NAIPKWHDLL PKSGDMVINM EWGNFRSSHL PLTEFDQALD AESLNPGEQV YEKLISGMYL GEIVRRVLLK MAEEASLFGD EVPPKLKIPF IIRTPYMSMM HCDRSPDLRT VGAKLKDILG VQNTSLKTRR LVVDVCDIVA KRAAHLAAAG IHGILKKLGR DVPNTDKQRT VIAVDGGLYE HYTIFAECVE STLRDMLGED VSSTIVIKLA KDGSGIGAAL LAAAHSQYRE AEEL //