ID   HXKL1_ARATH             Reviewed;         493 AA.
AC   Q9FZG4; A4VCN1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Hexokinase-like 1 protein;
DE            EC=2.7.1.1 {ECO:0000250|UniProtKB:P93834};
GN   OrderedLocusNames=At1g47840; ORFNames=T2E6.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista-Mercan V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C.,
RA   Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme.
CC       {ECO:0000250|UniProtKB:P93834}.
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:0000250|UniProtKB:P93834};
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:0000250|UniProtKB:P93834};
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:0000250|UniProtKB:P93834};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000250|UniProtKB:P93834}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000250|UniProtKB:P93834}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF99786.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC012463; AAF99786.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32221.1; -; Genomic_DNA.
DR   EMBL; BT030472; ABP88126.1; -; mRNA.
DR   RefSeq; NP_175220.2; NM_103682.4.
DR   AlphaFoldDB; Q9FZG4; -.
DR   SMR; Q9FZG4; -.
DR   STRING; 3702.Q9FZG4; -.
DR   iPTMnet; Q9FZG4; -.
DR   PaxDb; 3702-AT1G47840-1; -.
DR   ProteomicsDB; 232195; -.
DR   EnsemblPlants; AT1G47840.1; AT1G47840.1; AT1G47840.
DR   GeneID; 841200; -.
DR   Gramene; AT1G47840.1; AT1G47840.1; AT1G47840.
DR   KEGG; ath:AT1G47840; -.
DR   Araport; AT1G47840; -.
DR   TAIR; AT1G47840; HXK3.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_1_1; -.
DR   InParanoid; Q9FZG4; -.
DR   OMA; YPNFEGY; -.
DR   OrthoDB; 5481886at2759; -.
DR   PhylomeDB; Q9FZG4; -.
DR   BioCyc; ARA:AT1G47840-MONOMER; -.
DR   BRENDA; 2.7.1.1; 399.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:Q9FZG4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FZG4; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IDA:TAIR.
DR   GO; GO:0004340; F:glucokinase activity; IDA:TAIR.
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:SF63; HEXOKINASE-LIKE 1 PROTEIN-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; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
DR   Genevisible; Q9FZG4; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..493
FT                   /note="Hexokinase-like 1 protein"
FT                   /id="PRO_0000259633"
FT   DOMAIN          38..488
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          93..232
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          233..477
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         107
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         108
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         109
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         198
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
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         233
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         257
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         260
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         287
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         317
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
FT   BINDING         442
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LQ68"
SQ   SEQUENCE   493 AA;  53880 MW;  485C0BA6FBCDECF9 CRC64;
     MSLMFSSPVV TPALGSFTFS SRPRSNYIVM SAVRSNSAST CPILTKFQKD CATPTPYLRN
     VANAIADDMR DGLAVEGGGD LEMILTFVDA LPSGNEEGLF YALDLGGTNF RVRSVQLGGK
     KERVLATESE QISISQKLMI GTSEELFGFI ASKLANFVAK EKPGRFLLEE GRKRELGFTF
     SFPVKQTSID SGTLSKWTKG FKVSGMEGKN VVACLNEAME AHGLDMRVSA LVNDGVGTLA
     GARYWDEDVM VGVILGTGTN ACYVEQKHAI PKLRSKSSSG TTIINTEWGG FSKILPQTIF
     DLEMDETSLN PGEHLYEKMI SGMYLGEIVR RVLLHMCETS DLFGHFAPAK LSTPLALRTE
     HLCKMQEDNT DDLRDVGSIL YDFLDVEANM NARRRVVEVC DTVVKRGGRL AGAGIVAILE
     KIEKDTKRMG SGKRTVVAMD GALYEKYPQY RQYMQDALVE LLGHKLASHV AIKHTKDVSG
     LGAALLAATN SIY
//