HXK1_DROME
ID HXK1_DROME Reviewed; 465 AA.
AC Q9NFT9; Q6AWE1; Q9VBF1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Hexokinase type 1;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:A0A0K0JFP3};
GN Name=Hex-t1; Synonyms=Hex; ORFNames=CG33102;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-33 AND PHE-243.
RC STRAIN=DPF96e3_23.1, DPF96e3_3.0, DPF96e3_4.2, DPF96e3_74.2, DPF96e3_84.3,
RC HFL97e3_12, HFL97e3_13, HFL97e3_15, HFL97e3_16, HFL97e3_8, SC96e3_12.3,
RC SC96e3_19.4, VT97e3_1, VT97e3_39, VT97e3_41, ZIM(H)e3_38.4, ZIM(H)e3_39,
RC ZIM(S)e3_24, and ZIM(S)e3_35;
RX PubMed=11063694; DOI=10.1093/genetics/156.3.1191;
RA Duvernell D.D., Eanes W.F.;
RT "Contrasting molecular population genetics of four hexokinases in
RT Drosophila melanogaster, D. simulans and D. yakuba.";
RL Genetics 156:1191-1201(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-K;
RA Deobagkar D.D., Kulkarni G.V., Deobagkar D.N.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of various hexoses to hexose 6-
CC phosphate. {ECO:0000250|UniProtKB:A0A0K0JFP3}.
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:A0A0K0JFP3, ECO:0000255|PROSITE-
CC ProRule:PRU01084};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3};
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:0000250|UniProtKB:A0A0K0JFP3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3};
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:A0A0K0JFP3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3};
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:A0A0K0JFP3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:A0A0K0JFP3}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000250|UniProtKB:A0A0K0JFP3}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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; AF257590; AAG22891.1; -; Genomic_DNA.
DR EMBL; AF257591; AAG22893.1; -; Genomic_DNA.
DR EMBL; AF257592; AAG22895.1; -; Genomic_DNA.
DR EMBL; AF257593; AAG22897.1; -; Genomic_DNA.
DR EMBL; AF257594; AAG22899.1; -; Genomic_DNA.
DR EMBL; AF257595; AAG22901.1; -; Genomic_DNA.
DR EMBL; AF257596; AAG22903.1; -; Genomic_DNA.
DR EMBL; AF257597; AAG22905.1; -; Genomic_DNA.
DR EMBL; AF257598; AAG22907.1; -; Genomic_DNA.
DR EMBL; AF257599; AAG22909.1; -; Genomic_DNA.
DR EMBL; AF257600; AAG22911.1; -; Genomic_DNA.
DR EMBL; AF257601; AAG22913.1; -; Genomic_DNA.
DR EMBL; AF257602; AAG22915.1; -; Genomic_DNA.
DR EMBL; AF257603; AAG22917.1; -; Genomic_DNA.
DR EMBL; AF257604; AAG22919.1; -; Genomic_DNA.
DR EMBL; AF257605; AAG22921.1; -; Genomic_DNA.
DR EMBL; AF257606; AAG22923.1; -; Genomic_DNA.
DR EMBL; AF257607; AAG22925.1; -; Genomic_DNA.
DR EMBL; AF257608; AAG22927.1; -; Genomic_DNA.
DR EMBL; AJ271350; CAB72131.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56591.2; -; Genomic_DNA.
DR EMBL; BT015307; AAT94535.1; -; mRNA.
DR RefSeq; NP_788744.1; NM_176567.2.
DR AlphaFoldDB; Q9NFT9; -.
DR SMR; Q9NFT9; -.
DR IntAct; Q9NFT9; 1.
DR STRING; 7227.FBpp0084382; -.
DR PaxDb; Q9NFT9; -.
DR PRIDE; Q9NFT9; -.
DR DNASU; 117364; -.
DR EnsemblMetazoa; FBtr0085010; FBpp0084382; FBgn0042711.
DR GeneID; 117364; -.
DR KEGG; dme:Dmel_CG33102; -.
DR UCSC; CG33102-RA; d. melanogaster.
DR CTD; 117364; -.
DR FlyBase; FBgn0042711; Hex-t1.
DR VEuPathDB; VectorBase:FBgn0042711; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_5_3_1; -.
DR InParanoid; Q9NFT9; -.
DR OMA; VYMSSKC; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; Q9NFT9; -.
DR Reactome; R-DME-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70171; Glycolysis.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 117364; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 117364; -.
DR PRO; PR:Q9NFT9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0042711; Expressed in testis and 11 other tissues.
DR ExpressionAtlas; Q9NFT9; baseline and differential.
DR Genevisible; Q9NFT9; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0019158; F:mannokinase activity; IEA:RHEA.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
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; PS51748; HEXOKINASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..465
FT /note="Hexokinase type 1"
FT /id="PRO_0000197596"
FT DOMAIN 8..447
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 65..197
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 139..165
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 198..436
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 33
FT /note="N -> H (in strain: HFL97e3_12 and ZIM(S)e3_24)"
FT /evidence="ECO:0000269|PubMed:11063694"
FT VARIANT 243
FT /note="Y -> F (in strain: DPF96e3_3.0, DPF96e3_4.2,
FT DPF96e3_23.1, DPF96e3_74.2, VT97e3_41, SC96e3_12.3,
FT HFL97e3_8, HFL97e3_12, HFL97e3_15, ZIM(S)e3_24 and
FT ZIM(S)e3_35)"
FT /evidence="ECO:0000269|PubMed:11063694"
SQ SEQUENCE 465 AA; 52260 MW; 67B611920D56B6DD CRC64;
MANTFNPEED FPEVYKVCKL FNPSIDDLEK IKNAMDREIT MGLSRDHHDR STVPCHLSYV
QDLPTGRERG QFLALEMMPT NCRIMLVKFS SERDIYTSSK CVIMPHTVAA GRGTEVFTFL
ATSIANFVKE KKVDKDNLPL GIAFAFTLKK LALDVGILVS WTKEFGAQGA IGKDVVQLLR
DALAKFPEIS VDVMGIINVG AGSLLALCWA QPDTRIGLIM GSIANSCYVE RVERCETYEG
DEYRKLMIIN SDWAHFGDTG QLDFIRNEYD RQLDTESINP GTRIYEKFSG ALCMGELVRI
IVLRLMKSGA IFAEDRRDYI GIQWKLDMVS LIEIVSDPPG VYTKAQEVMD KFRIRHCKER
DLAALKYICD TVTNRAAMLV ASGVSCLIDR MRLPQISIAV DGGIYRLHPT FSTVLNKYTR
LLADPNYNFE FVITQDSCGV GAAIMAGMAH ANKYKTDAKL FTMDY
