ID Q59FD4_HUMAN Unreviewed; 949 AA. AC Q59FD4; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 02-SEP-2026, entry version 121. DE RecName: Full=hexokinase {ECO:0000256|ARBA:ARBA00012324, ECO:0000256|PROSITE-ProRule:PRU01084}; DE EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324, ECO:0000256|PROSITE-ProRule:PRU01084}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92763.1}; RN [1] {ECO:0000313|EMBL:BAD92763.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:BAD92763.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose + ATP = D-glucose 6-phosphate + ADP + 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:0000256|ARBA:ARBA00048160}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; CC Evidence={ECO:0000256|ARBA:ARBA00048160}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; CC EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00044613}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; CC Evidence={ECO:0000256|ARBA:ARBA00044613}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 1/4. CC {ECO:0000256|ARBA:ARBA00004888}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|ARBA:ARBA00005028}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004318}; Peripheral CC membrane protein {ECO:0000256|ARBA:ARBA00004318}. CC -!- SIMILARITY: Belongs to the hexokinase family. CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|PROSITE-ProRule:PRU01084}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01084}. 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; AB209526; BAD92763.1; -; mRNA. DR RefSeq; NP_000179.2; NM_000188.3. DR AlphaFoldDB; Q59FD4; -. DR SMR; Q59FD4; -. DR IntAct; Q59FD4; 1. DR PeptideAtlas; Q59FD4; -. DR DNASU; 3098; -. DR GeneID; 3098; -. DR KEGG; hsa:3098; -. DR ClinPGx; PA29300; -. DR CTD; 3098; -. DR DisGeNET; 3098; -. DR OrthoDB; 419537at2759; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR BioGRID-ORCS; 3098; 16 hits in 1175 CRISPR screens. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0005536; F:D-glucose binding; IEA:InterPro. DR GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC. 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; cd24124; ASKHA_NBD_HK1_meta_rpt1; 1. DR CDD; cd24127; ASKHA_NBD_HK1_meta_rpt2; 1. DR FunFam; 3.30.420.40:FF:000015; Hexokinase 1; 1. DR FunFam; 3.40.367.20:FF:000001; Hexokinase 1; 1. DR FunFam; 3.30.420.40:FF:000555; Hexokinase-1; 1. DR FunFam; 3.40.367.20:FF:000020; Hexokinase-1; 1. DR Gene3D; 3.30.420.40; -; 2. DR Gene3D; 3.40.367.20; -; 2. 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:SF10; HEXOKINASE-1; 1. DR Pfam; PF00349; Hexokinase_1; 2. DR Pfam; PF03727; Hexokinase_2; 2. DR PRINTS; PR00475; HEXOKINASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 4. DR PROSITE; PS00378; HEXOKINASE_1; 2. DR PROSITE; PS51748; HEXOKINASE_2; 2. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU01084}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|PROSITE- KW ProRule:PRU01084}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU01084}; Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU01084}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU01084}. FT DOMAIN 54..251 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 258..491 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT DOMAIN 502..699 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 706..939 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD92763.1" SQ SEQUENCE 949 AA; 105804 MW; 54972BD394467EA3 CRC64; GAAEQPPEDH GSPGLRRTDR PHACRPATPT ASMIAAQLLA YYFTELKDDQ VKKIDKYLYA MRLSDETLID IMTRFRKEMK NGLSRDFNPT ATVKMLPTFV RSIPDGSEKG DFIALDLGGS SFRILRVQVN HEKNQNVHME SEVYDTPENI VHGSGSQLFD HVAECLGDFM EKRKIKDKKL PVGFTFSFPC QQSKIDEAIL ITWTKRFKAS GVEGADVVKL LNKAIKKRGD YDANIVAVVN DTVGTMMTCG YDDQHCEVGL IIGTGTNACY MEELRHIDLV EGDEGRMCIN TEWGAFGDDG SLEDIRTEFD REIDRGSLNP GKQLFEKMVS GMYLGELVRL ILVKMAKEGL LFEGRITPEL LTRGKFNTSD VSAIEKNKEG LHNAKEILTR LGVEPSDDDC VSVQHVCTIV SFRSANLVAA TLGAILNRLR DNKGTPRLRT TVGVDGSLYK THPQYSRRFH KTLRRLVPDS DVRFLLSESG SGKGAAMVTA VAYRLAEQHR QIEETLAHFH LTKDMLLEVK KRMRAEMELG LRKQTHNNAV VKMLPSFVRR TPDGTENGDF LALDLGGTNF RVLLVKIRSG KKRTVEMHNK IYAIPIEIMQ GTGEELFDHI VSCISDFLDY MGIKGPRMPL GFTFSFPCQQ TSLDAGILIT WTKGFKATDC VGHDVVTLLR DAIKRREEFD LDVVAVVNDT VGTMMTCAYE EPTCEVGLIV GTGSNACYME EMKNVEMVEG DQGQMCINME WGAFGDNGCL DDIRTHYDRL VDEYSLNAGK QRYEKMISGM YLGEIVRNIL IDFTKKGFLF RGQISETLKT RGIFETKFLS QIESDRLALL QVRAILQQLG LNSTCDDSIL VKTVCGVVSR RAAQLCGAGM AAVVDKIREN RGLDRLNVTV GVDGTLYKLH PHFSRIMHQT VKELSPKCNV SFLLSEDGSG KGAALITAVG VRLRTEASS //