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Database: UniProt/SWISS-PROT
Entry: HXK1_SCHPO
LinkDB: HXK1_SCHPO
Original site: HXK1_SCHPO 
ID   HXK1_SCHPO              Reviewed;         484 AA.
AC   Q09756;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Hexokinase-1 {ECO:0000303|PubMed:8549830};
DE            EC=2.7.1.1 {ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
GN   Name=hxk1 {ECO:0000303|PubMed:8549830}; ORFNames=SPAC24H6.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8549830; DOI=10.1016/0014-5793(95)01451-9;
RA   Petit T., Blazquez M.A., Gancedo C.;
RT   "Schizosaccharomyces pombe possesses an unusual and a conventional
RT   hexokinase: biochemical and molecular characterization of both
RT   hexokinases.";
RL   FEBS Lett. 378:185-189(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-213.
RX   PubMed=9790975; DOI=10.1006/bbrc.1998.9538;
RA   Petit T., Herrero P., Gancedo C.;
RT   "A mutation Ser213/Asn in the hexokinase 1 from Schizosaccharomyces pombe
RT   increases its affinity for glucose.";
RL   Biochem. Biophys. Res. Commun. 251:714-719(1998).
CC   -!- FUNCTION: Catalyzes the phosphorylation of hexose (six-carbon sugars)
CC       to hexose 6-phosphate (PubMed:8549830, PubMed:9790975). Phosphorylates
CC       D-fructose, D-mannose and, to a lower extent, D-glucose
CC       (PubMed:8549830, PubMed:9790975). Compared to hxk2, has low affinity
CC       for D-glucose (PubMed:8549830, PubMed:9790975).
CC       {ECO:0000269|PubMed:8549830, ECO:0000269|PubMed:9790975}.
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:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC         Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
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:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
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:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000269|PubMed:9790975, ECO:0000305|PubMed:8549830};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.5 mM for D-fructose {ECO:0000269|PubMed:9790975};
CC         KM=9.4 mM for D-glucose {ECO:0000269|PubMed:9790975};
CC         KM=0.2 mM for D-mannose {ECO:0000269|PubMed:9790975};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000305|PubMed:8549830}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000305|PubMed:8549830}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P19367}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; X92894; CAA63487.1; -; mRNA.
DR   EMBL; CU329670; CAA90848.1; -; Genomic_DNA.
DR   PIR; S68694; S68694.
DR   RefSeq; NP_592948.1; NM_001018349.2.
DR   AlphaFoldDB; Q09756; -.
DR   SMR; Q09756; -.
DR   BioGRID; 279088; 7.
DR   STRING; 284812.Q09756; -.
DR   iPTMnet; Q09756; -.
DR   SwissPalm; Q09756; -.
DR   MaxQB; Q09756; -.
DR   PaxDb; 4896-SPAC24H6-04-1; -.
DR   EnsemblFungi; SPAC24H6.04.1; SPAC24H6.04.1:pep; SPAC24H6.04.
DR   GeneID; 2542634; -.
DR   KEGG; spo:SPAC24H6.04; -.
DR   PomBase; SPAC24H6.04; hxk1.
DR   VEuPathDB; FungiDB:SPAC24H6.04; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_2_1; -.
DR   InParanoid; Q09756; -.
DR   OMA; ADCVQQF; -.
DR   PhylomeDB; Q09756; -.
DR   BRENDA; 2.7.1.1; 5613.
DR   Reactome; R-SPO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-70171; Glycolysis.
DR   SABIO-RK; Q09756; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:Q09756; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0008865; F:fructokinase activity; IDA:PomBase.
DR   GO; GO:0004340; F:glucokinase activity; IDA:PomBase.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IDA:PomBase.
DR   GO; GO:0019158; F:mannokinase activity; IDA:PomBase.
DR   GO; GO:0061621; P:canonical glycolysis; IC:PomBase.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR   GO; GO:0006000; P:fructose metabolic process; IDA:PomBase.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IDA:PomBase.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0006013; P:mannose metabolic process; IDA:PomBase.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; TAS:PomBase.
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   1: Evidence at protein level;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..484
FT                   /note="Hexokinase-1"
FT                   /id="PRO_0000197609"
FT   DOMAIN          25..465
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          79..212
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          213..454
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         90..95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         160..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         177..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         213..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         307..308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         344..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   BINDING         419..423
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P35557"
FT   MUTAGEN         213
FT                   /note="S->N: Increased affinity for D-glucose."
FT                   /evidence="ECO:0000269|PubMed:9790975"
SQ   SEQUENCE   484 AA;  53598 MW;  165500F19E6BBB0F CRC64;
     MSLHDAYHWP SRTPSRKGSN IKLNKTLQDH LDELEEQFTI PTELLHRVTD RFVSELYKGL
     TTNPGDVPMV PTWIIGTPDG NEHGSYLALD LGGTNLRVCA VEVQGNGKFD ITQSKYRLPQ
     ELKVGTREAL FDYIADCIKK FVEEVHPGKS QNLEIGFTFS YPCVQRSIND ASLVAWTKGF
     DIDGVEGESV GPLLSAALKR VGCNNVRLNA ILSDTTGTLV ASNYASPGTE IGVIFGTGCN
     ACYIEKFSEI PKLHKYDFPE DMNMIINCEW CDFDNQHVVL PRTKYDVAID EESPRPGLQT
     YEKMIAGCYL GDILRRILLD LYEQGALFNG QDVTKIRDPL AMDTSVLSAI EVDPFENLDE
     TQTLFEETYG LKTTEEERQF IRRACELIGT RSARLSACGV CALVRKMNKP SMIVGTDGSV
     YNLYPRFKDR LAQAFKDILG EEIGSKVVTI PAEDGSGVGA ALVSALEAKG KALTSDILAE
     HLKN
//
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