HXK2_DROME
ID HXK2_DROME Reviewed; 486 AA.
AC Q9NFT7; Q95U08; Q9NFT8; Q9VBF1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Hexokinase type 2;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:A0A0K0JFP3};
GN Name=Hex-t2; Synonyms=Hex; ORFNames=CG32849;
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 ASN-194; THR-252; ASN-380;
RP ASN-484 AND ILE-486.
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] OF 2-486.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG22892.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22900.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22902.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22906.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22908.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22914.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22918.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22924.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG22928.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL13623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB67701.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=CAB72132.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
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DR EMBL; AF257590; AAG22892.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257591; AAG22894.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257592; AAG22896.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257593; AAG22898.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257594; AAG22900.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257595; AAG22902.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257596; AAG22904.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257597; AAG22906.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257598; AAG22908.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257599; AAG22910.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257600; AAG22912.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257601; AAG22914.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257602; AAG22916.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257603; AAG22918.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257604; AAG22920.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257605; AAG22922.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257606; AAG22924.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257607; AAG22926.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF257608; AAG22928.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ271350; CAB67701.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ271350; CAB72132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAN14073.2; -; Genomic_DNA.
DR EMBL; AY058394; AAL13623.1; ALT_INIT; mRNA.
DR RefSeq; NP_733151.2; NM_170272.3.
DR AlphaFoldDB; Q9NFT7; -.
DR SMR; Q9NFT7; -.
DR IntAct; Q9NFT7; 1.
DR STRING; 7227.FBpp0084383; -.
DR PaxDb; Q9NFT7; -.
DR PRIDE; Q9NFT7; -.
DR DNASU; 43191; -.
DR EnsemblMetazoa; FBtr0085011; FBpp0084383; FBgn0042710.
DR GeneID; 43191; -.
DR KEGG; dme:Dmel_CG32849; -.
DR UCSC; CG32849-RA; d. melanogaster.
DR CTD; 43191; -.
DR FlyBase; FBgn0042710; Hex-t2.
DR VEuPathDB; VectorBase:FBgn0042710; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_5_3_1; -.
DR InParanoid; Q9NFT7; -.
DR OMA; HLRYICE; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; Q9NFT7; -.
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; 43191; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43191; -.
DR PRO; PR:Q9NFT7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0042710; Expressed in testis and 10 other tissues.
DR ExpressionAtlas; Q9NFT7; baseline and differential.
DR Genevisible; Q9NFT7; 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:0004396; F:hexokinase activity; ISS:FlyBase.
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:0006000; P:fructose metabolic process; ISS:FlyBase.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; ISS:FlyBase.
DR GO; GO:0006096; P:glycolytic process; ISS:FlyBase.
DR GO; GO:0006013; P:mannose metabolic process; ISS:FlyBase.
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 2: Evidence at transcript level;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..486
FT /note="Hexokinase type 2"
FT /id="PRO_0000197597"
FT DOMAIN 36..477
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 93..225
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 167..193
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 226..466
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VARIANT 194
FT /note="S -> N (in strain: HFL97e3_15)"
FT /evidence="ECO:0000269|PubMed:11063694"
FT VARIANT 252
FT /note="S -> T (in strain: ZIM(S)e3_24)"
FT /evidence="ECO:0000269|PubMed:11063694"
FT VARIANT 380
FT /note="S -> N (in strain: SC96e3_12.3 and ZIM(S)e3_35)"
FT /evidence="ECO:0000269|PubMed:11063694"
FT VARIANT 484
FT /note="S -> N (in strain: DPF96e3_23.1, SC96e3_12.3,
FT HFL97e3_8, HFL97e3_12, HFL97e3_16, ZIM(S)e3_24 and
FT ZIM(S)e3_35)"
FT /evidence="ECO:0000269|PubMed:11063694"
FT VARIANT 486
FT /note="L -> I (in strain: DPF96e3_23.1, SC96e3_12.3,
FT HFL97e3_8, HFL97e3_12, HFL97e3_16 and ZIM(S)e3_24)"
FT /evidence="ECO:0000269|PubMed:11063694"
FT CONFLICT 167
FT /note="A -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53486 MW; 79D011558E1E5ED6 CRC64;
MRKSTRLLTH SLFGPVFKIL FHNKTVCGGC NRKMPSLVNT EIEAAVKGFL IDQEKMTEVV
ERMTKEIKMG LAKDTHARAV IKCFVSHVQD LPTGKERGKY LALDLGGSNF RVLLVNLISN
SDVETMSKGY NFPQTLMSGS GKALFDFLAE CLSEFCHSHG LENESLALGF TFSFPLQQQG
LSKGILVAWT KGFSCEGVVG KNVVSLLQEA IDRRGDLKIN TVAILNDTVG TLMSCAFYHP
NCRIGLIVGT GSNACYVEKT VNAECFEGYQ TSPKPSMIIN CEWGAFGDNG VLEFVRTSYD
KAVDKVTPNP GKQTFEKCIS GMYMGELVRL VITDMIAKGF MFHGIISEKI QERWSFKTAY
ISDVESDAPG EYRNCNKVLS ELGILGCQEP DKEALRYICE AVSSRSAKLC ACGLVTIINK
MNINEVAIGI DGSVYRFHPK YHDMLQYHMK KLLKPGVKFE LVVSEDGSGR GAALVAATAV
QAKSKL
