GenomeNet

Database: UniProt/SWISS-PROT
Entry: HXK2_DROME
LinkDB: HXK2_DROME
Original site: 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   30-AUG-2017, entry version 134.
DE   RecName: Full=Hexokinase type 2;
DE            EC=2.7.1.1;
GN   Name=Hex-t2; Synonyms=Hex; ORFNames=CG32849;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-194; THR-252;
RP   ASN-380; ASN-484 AND ILE-486.
RC   STRAIN=DPF96e3_23.1, DPF96e3_3.0, DPF96e3_4.2, DPF96e3_74.2,
RC   DPF96e3_84.3, HFL97e3_12, HFL97e3_13, HFL97e3_15, HFL97e3_16,
RC   HFL97e3_8, SC96e3_12.3, SC96e3_19.4, VT97e3_1, VT97e3_39, VT97e3_41,
RC   ZIM(H)e3_38.4, ZIM(H)e3_39, ZIM(S)e3_24, and ZIM(S)e3_35;
RX   PubMed=11063694;
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000255|PROSITE-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};
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   ProteinModelPortal; Q9NFT7; -.
DR   SMR; Q9NFT7; -.
DR   IntAct; Q9NFT7; 1.
DR   STRING; 7227.FBpp0084383; -.
DR   PaxDb; Q9NFT7; -.
DR   PRIDE; Q9NFT7; -.
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   eggNOG; KOG1369; Eukaryota.
DR   eggNOG; COG5026; LUCA.
DR   GeneTree; ENSGT00390000017159; -.
DR   InParanoid; Q9NFT7; -.
DR   KO; K00844; -.
DR   OMA; LMSCAFY; -.
DR   OrthoDB; EOG091G08MD; -.
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-70153; Glucose transport.
DR   Reactome; R-DME-70171; Glycolysis.
DR   UniPathway; UPA00242; -.
DR   GenomeRNAi; 43191; -.
DR   PRO; PR:Q9NFT7; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0042710; -.
DR   ExpressionAtlas; Q9NFT7; differential.
DR   Genevisible; Q9NFT7; DM.
DR   GO; GO:0005829; C:cytosol; 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; 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: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; 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   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Glycolysis; Kinase;
KW   Nucleotide-binding; Polymorphism; Reference proteome; Transferase.
FT   CHAIN         1    486       Hexokinase type 2.
FT                                /FTId=PRO_0000197597.
FT   DOMAIN       36    477       Hexokinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   REGION       93    225       Hexokinase small subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      167    193       Glucose-binding. {ECO:0000255}.
FT   REGION      226    466       Hexokinase large subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   BINDING     128    128       ATP.
FT   VARIANT     194    194       S -> N (in strain: HFL97e3_15).
FT                                {ECO:0000269|PubMed:11063694}.
FT   VARIANT     252    252       S -> T (in strain: ZIM(S)e3_24).
FT                                {ECO:0000269|PubMed:11063694}.
FT   VARIANT     380    380       S -> N (in strain: SC96e3_12.3 and
FT                                ZIM(S)e3_35).
FT                                {ECO:0000269|PubMed:11063694}.
FT   VARIANT     484    484       S -> N (in strain: DPF96e3_23.1,
FT                                SC96e3_12.3, HFL97e3_8, HFL97e3_12,
FT                                HFL97e3_16, ZIM(S)e3_24 and ZIM(S)e3_35).
FT                                {ECO:0000269|PubMed:11063694}.
FT   VARIANT     486    486       L -> I (in strain: DPF96e3_23.1,
FT                                SC96e3_12.3, HFL97e3_8, HFL97e3_12,
FT                                HFL97e3_16 and ZIM(S)e3_24).
FT                                {ECO:0000269|PubMed:11063694}.
FT   CONFLICT    167    167       A -> P (in Ref. 1). {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
//
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