HXK1_SOLTU
ID HXK1_SOLTU Reviewed; 498 AA.
AC O64390;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Hexokinase-1;
DE EC=2.7.1.1 {ECO:0000269|PubMed:10482667};
DE AltName: Full=StHK1;
GN Name=HXK1; Synonyms=HXK;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RA Clericus M., Heins L., Schmitz U.K.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=10482667; DOI=10.1104/pp.121.1.123;
RA Veramendi J., Roessner U., Renz A., Willmitzer L., Trethewey R.N.;
RT "Antisense repression of hexokinase 1 leads to an overaccumulation of
RT starch in leaves of transgenic potato plants but not to significant changes
RT in tuber carbohydrate metabolism.";
RL Plant Physiol. 121:123-134(1999).
CC -!- FUNCTION: Fructose and glucose phosphorylating enzyme. May be involved
CC in the phosphorylation of glucose during the export from plastids to
CC cytosol. Seems neither to be involved in cell sugar sensing nor in
CC carbohydrate metabolism in tuber. {ECO:0000269|PubMed:10482667}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:10482667};
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:0000269|PubMed:10482667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000269|PubMed:10482667};
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:0000269|PubMed:10482667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:10482667};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.033 mM for glucose {ECO:0000269|PubMed:10482667};
CC KM=1.470 mM for fructose {ECO:0000269|PubMed:10482667};
CC KM=0.029 mM for mannose {ECO:0000269|PubMed:10482667};
CC Vmax=349 nmol/min/mg enzyme with glucose as substrate
CC {ECO:0000269|PubMed:10482667};
CC Vmax=523 nmol/min/mg enzyme with fructose as substrate
CC {ECO:0000269|PubMed:10482667};
CC Vmax=221 nmol/min/mg enzyme with mannose as substrate
CC {ECO:0000269|PubMed:10482667};
CC Note=Measured in yeast lacking glucose and hexose kinase activity.;
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:10482667}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000305|PubMed:10482667}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young and mature leaves, stems, roots,
CC stolons, and developing and mature tubers.
CC {ECO:0000269|PubMed:10482667}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; X94302; CAA63966.1; -; mRNA.
DR PIR; T07384; T07384.
DR RefSeq; NP_001305619.1; NM_001318690.1.
DR AlphaFoldDB; O64390; -.
DR SMR; O64390; -.
DR STRING; 4113.PGSC0003DMT400006474; -.
DR PRIDE; O64390; -.
DR GeneID; 102604144; -.
DR KEGG; sot:102604144; -.
DR eggNOG; KOG1369; Eukaryota.
DR InParanoid; O64390; -.
DR BRENDA; 2.7.1.1; 5757.
DR SABIO-RK; O64390; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; O64390; baseline.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0001678; P:cellular glucose homeostasis; 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 InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
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..498
FT /note="Hexokinase-1"
FT /id="PRO_0000197615"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..488
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 89..228
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 171..197
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 229..477
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 101..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 498 AA; 54130 MW; D7F598CBB12762E4 CRC64;
MKKVTVGAAV VGAAAVCAVA ALIVNHRMRK SSKWGRAMAI LREFEEKCKT QDAKLKQVAD
AMTVEMHAGL ASEGGQSSRC LSPMSIISQL VMKLGVFYAL DLGGTNFRVL RVQLGGKDGG
IIHQEFAEAS IPPSLMVGTS DALFDYIAAE LAKFVAAEEE KFHQPPGKQR ELGFHLLIPS
NADFNNSGTI MRWTKGFSID DAVGQDVVGE LTKAMKEKVL DMRVSALVND TVGTLAGGKY
TQKDVAVAVI LGTGTNAAYV ERVQAIPKWH GPVPKSGEMV INMEWGNFRS SHLPLTEYDH
ALDNESLNPA EQIFEKMTSG MYLGEILRRV LTRVAEEVLA FLAMRSLQSL KDSFVLRTPD
MSAMHHDTSP DLKVVGEKLK DILEISNTSL KTRKLVLSLC NIVATRGARL DAAGVLGILK
KMGRDTPKQG GSERTVIAMD GGLYEHYTEY RMCLENSLKD LLGEELATSI VFVHSNDGSG
IGAALLRASH SMYLEDQA
