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 03-AUG-2022, entry version 154.
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; 4896.SPAC24H6.04.1; -.
DR iPTMnet; Q09756; -.
DR SwissPalm; Q09756; -.
DR MaxQB; Q09756; -.
DR PaxDb; Q09756; -.
DR PRIDE; Q09756; -.
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; IAINCEW; -.
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:0001678; P:cellular glucose homeostasis; 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:0006013; P:mannose metabolic process; IDA:PomBase.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; TAS:PomBase.
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 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
