ID   HXK_SCHOC               Reviewed;         478 AA.
AC   P50506;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Hexokinase;
DE            EC=2.7.1.1 {ECO:0000250|UniProtKB:P33284};
GN   Name=HXK;
OS   Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX   NCBI_TaxID=27300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 2322 / CBS 819 / JCM 8123 / NBRC 1841 / NRRL Y-10 / BCRC 22052;
RX   PubMed=7614556; DOI=10.1007/bf00352102;
RA   Rose M.;
RT   "Molecular and biochemical characterization of the hexokinase from the
RT   starch-utilizing yeast Schwanniomyces occidentalis.";
RL   Curr. Genet. 27:330-338(1995).
CC   -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC       and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC       fructose 6-phosphate, respectively). Mediates the initial step of
CC       glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-
CC       phosphate. {ECO:0000250|UniProtKB:P33284}.
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:P33284};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
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:P33284};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
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:P33284};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000250|UniProtKB:P33284}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000250|UniProtKB:P33284}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P33284}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; S78714; AAB34892.1; -; Genomic_DNA.
DR   PIR; S57203; S57203.
DR   AlphaFoldDB; P50506; -.
DR   SMR; P50506; -.
DR   PRIDE; P50506; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
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:0006013; P:mannose metabolic process; IEA:UniProt.
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   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..478
FT                   /note="Hexokinase"
FT                   /id="PRO_0000197606"
FT   DOMAIN          21..465
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          75..208
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          151..177
FT                   /note="Glucose-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          209..454
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  53067 MW;  080D5F9134478ABA CRC64;
     MVHLGPKPPQ HRKGSFLDVP EYLLKELTEL EGLLTVSGET LRKITDHFIS ELEKGLSKQG
     GNIPMIPGWV MDFPTGKEMG DYLAIDLGGT NLRVVLVKLG GNRDFDTTQS KFALPENMRT
     AKSEELWEFI AECLQKFVEE EFRNGVLSNL PLGFTFSYPA SQGSINEGYL QRWTKGFDIE
     GVEGHDVVPM LQAAIEKRKV PIEVVALIND TTGTLVASMY TDPEAKMGLF SGTGCNGAYY
     DVVDNIPKLE GKVPDDIKSS SPMAINCEYG AFDNEHIILP RTKYDIQIDE ESPRPGQQAF
     EKMISGYYLG EVLRLILLDL TSKQLIFKDQ DLSKLQVPFI LDTSIPARIE EDPFENLSDV
     QELFQEILGI QTTSPERKII RRLAELIGER SARLSICGIA AICKKRGYKT AHCAADGSVY
     NKYPGFKERA AKGLRDIFQW ESEEDPIVIV PAEDGLGAGA AIIAALTEKR LKDGLPLV