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Database: UniProt
Entry: N1P4S9_YEASC
LinkDB: N1P4S9_YEASC
Original site: N1P4S9_YEASC 
ID   N1P4S9_YEASC            Unreviewed;       485 AA.
AC   N1P4S9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=CENPK1137D_3329 {ECO:0000313|EMBL:EIW10711.1};
OS   Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW10711.1};
RN   [1] {ECO:0000313|EMBL:EIW10711.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW10711.1};
RA   Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA   Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA   Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA   Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT   "De novo sequencing, assembly and analysis of the genome of the laboratory
RT   strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT   biotechnology.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001397};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000256|ARBA:ARBA00001397};
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   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR   EMBL; CM001527; EIW10711.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1P4S9; -.
DR   SMR; N1P4S9; -.
DR   HOGENOM; CLU_014393_5_2_1; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000013192; Chromosome VI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 1.10.287.1250; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
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:SF16; HEXOKINASE TYPE 1-RELATED; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362007};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          27..221
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          227..469
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   485 AA;  53738 MW;  AF5C9DA8F17BC3D0 CRC64;
     MVHLGPKKPQ ARKGSMADVP KELMDEIHQL EDMFTVDSET LRKVVKHFID ELNKGLTKKG
     GNIPMIPGWV MEFPTGKESG NYLAIDLGGT NLRVVLVKLS GNHTFDTTQS KYKLPHDMRT
     TKHQEELWSF IADSLKDFMV EQELLNTKDT LPLGFTFSYP ASQNKINEGI LQRWTKGFDI
     PNVEGHDVVP LLQNEISKRE LPIEIVALIN DTVGTLIASY YTDPETKMGV IFGTGVNGAF
     YDVVSDIEKL EGKLADDIPS NSPMAINCEY GSFDNEHLVL PRTKYDVAVD EQSPRPGQQA
     FEKMTSGYYL GELLRLVLLE LNEKGLMLKD QDLSKLKQPY IMDTSYPARI EDDPFENLED
     TDDIFQKDFG VKTTLPERKL IRRLCELIGT RAARLAVCGI AAICQKRGYK TGHIAADGSV
     YNKYPGFKEA AAKGLRDIYG WTGDASKDPI TIVPAEDGSG AGAAVIAALS EKRIAEGKSL
     GIIGA
//
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