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HXK1_TOBAC
ID   HXK1_TOBAC              Reviewed;         497 AA.
AC   Q9SEK2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Hexokinase-1;
DE            EC=2.7.1.1 {ECO:0000250|UniProtKB:Q6Q8A5};
DE   AltName: Full=NtHxK1;
GN   Name=HXK1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10561488; DOI=10.1016/s0014-5793(99)01417-9;
RA   Wiese A., Groener F., Sonnewald U., Deppner H., Lerchl J., Fluegge U.I.,
RA   Weber A.;
RT   "Spinach hexokinase I is located in the outer envelope membrane of
RT   plastids.";
RL   FEBS Lett. 461:13-18(1999).
CC   -!- FUNCTION: Fructose and glucose phosphorylating enzyme.
CC       {ECO:0000250|UniProtKB:Q6Q8A5}.
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:Q6Q8A5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000250|UniProtKB:Q6Q8A5};
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:Q6Q8A5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000250|UniProtKB:Q6Q8A5};
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:Q6Q8A5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000250|UniProtKB:Q6Q8A5};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000250|UniProtKB:Q6Q8A5}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000250|UniProtKB:Q6Q8A5}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; AF118133; AAF18585.1; -; mRNA.
DR   RefSeq; NP_001312563.1; NM_001325634.1.
DR   AlphaFoldDB; Q9SEK2; -.
DR   SMR; Q9SEK2; -.
DR   STRING; 4097.Q9SEK2; -.
DR   ProMEX; Q9SEK2; -.
DR   GeneID; 107797523; -.
DR   KEGG; nta:107797523; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000084051; Unplaced.
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; IPR019807; Hexokinase_BS.
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; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   2: Evidence at transcript 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..497
FT                   /note="Hexokinase-1"
FT                   /id="PRO_0000197618"
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..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..476
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   497 AA;  53740 MW;  05F6825652C28F70 CRC64;
     MKKATVGAAV IGAATVCAVA ALIVNHRMRK SSKWARAMAI LREFEEKCGT PDAKLKQVAD
     AMTVEMHAGL ASEGGSKLKM LITYVDNLPT GDEAGVFYAL DLGGTNFRVL RVQLGGKDGG
     IVHQEFAEAS IPPNLMVGTS EALFDYIAAE LAKFVNEEGE KFQQPPGKQR ELGFTFSFPV
     MQTSINSGTI MRWTKGFSID DAVGQDVVGE LAKAMKRKGV DMRVSALVND TVGTLAGGKY
     THNDVAVAVI LGTGTNAAYV ERVQAIPKWH GPVPKSGEMV INMEWGNFRS SHLPLTQYDH
     ALDTNSLNPG DQIFEKMTSG MYLGEILRRV LLRVAEEAGI FGDEVPPKLK SPFVLRTPDM
     SAMHHDASSD LRVVGDKLKD ILEISNTSLK TRRLVIELCN IVATRGARLA AAGVLGILKK
     MGRDTPRQGG LEKTVVAMDG GLYEHYTEYR MCLENTLKEL LGDELATSIV FEHSNDGSGI
     GAALLAASNS MYLEDKS
 
 
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