HXK1_SPIOL
ID HXK1_SPIOL Reviewed; 498 AA.
AC Q9SEK3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Hexokinase-1;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:Q6Q8A5};
DE AltName: Full=SoHxK1;
GN Name=HXK1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
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:0000269|PubMed:10561488}; Single-pass membrane protein
CC {ECO:0000269|PubMed:10561488}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; AF118132; AAF18584.1; -; mRNA.
DR AlphaFoldDB; Q9SEK3; -.
DR SMR; Q9SEK3; -.
DR PRIDE; Q9SEK3; -.
DR OrthoDB; 1153545at2759; -.
DR BRENDA; 2.7.1.1; 5812.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Glycolysis; Kinase; Membrane; Nucleotide-binding;
KW Plastid; Plastid outer membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..498
FT /note="Hexokinase-1"
FT /id="PRO_0000197617"
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 498 AA; 54135 MW; B4C91FF7DB26FE29 CRC64;
MRKAAVGAAV VCTAAVCAAA AVLVRQRMKS SSKWGRVMAI LKELDDNCGT PLGKLRQVAD
AMTVEMHAGL ASEGASKLKM LISYVDNLPT GDEHGLFYAL DLGGTNFRVL RVKLGGKEKR
VVEQEFDEVS IPPELMVGTS EQLFDYIAEA LAKFVATESE GLHPEPNKQR ELGFTFSFPV
KQTSIASGTL IRWTKGFNIE DTVGEDVVAE LTKAMLRKGV DMRVTALVND TVGTLAGGRY
YKEDVIAAVI LGTGTNAAYV ERASAIHKWH GPLPKSGEMV INMEWGNFRS SYLPLTEYDI
ALDEESLNPG EQIFEKMISG MYLGEIVRRV LYRMADEASL FGDTVPSKLK TPFILRTPDM
SAMHHDTSPD LKVVASKLKD VLGIPNSSLK VRKIIVDVCD VIASRGACIS AAGILGIIKK
LGRDTLKQGE NQKSVIALDG GLFEHYAKFR ECMEDSLKEL LGDEVAETIV IEHSNDGSGI
GAALLAASHS QYLEEDES
