ID Q7ZUM3_DANRE Unreviewed; 918 AA. AC Q7ZUM3; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Hexokinase-1 {ECO:0000256|ARBA:ARBA00044081}; DE EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324}; DE AltName: Full=Hexokinase type I {ECO:0000256|ARBA:ARBA00044308}; GN Name=hk1 {ECO:0000313|EMBL:AAH48065.1, ECO:0000313|RefSeq:NP_998417.1, GN ECO:0000313|ZFIN:ZDB-GENE-040426-2848}; GN Synonyms=im:7148527 {ECO:0000313|RefSeq:NP_998417.1}, wu:fc16e02 GN {ECO:0000313|RefSeq:NP_998417.1}, wu:fc21e02 GN {ECO:0000313|RefSeq:NP_998417.1}, wu:fq14b11 GN {ECO:0000313|RefSeq:NP_998417.1}, zgc:55790 GN {ECO:0000313|RefSeq:NP_998417.1}, zgc:77618 GN {ECO:0000313|RefSeq:NP_998417.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH48065.1}; RN [1] {ECO:0000313|EMBL:AAH48065.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=AB {ECO:0000313|EMBL:AAH48065.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:AAH48065.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=19087890; RA Gonzalez-Alvarez R., Ortega-Cuellar D., Hernandez-Mendoza A., RA Moreno-Arriola E., Villasenor-Mendoza K., Galvez-Mariscal A., RA Perez-Cruz M.E., Morales-Salas I., Velazquez-Arellano A.; RT "The hexokinase gene family in the zebrafish: structure, expression, RT functional and phylogenetic analysis."; RL Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 152:189-195(2009). RN [3] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [4] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=23659367; RA Seiliez I., Medale F., Aguirre P., Larquier M., Lanneretonne L., RA Alami-Durante H., Panserat S., Skiba-Cassy S.; RT "Postprandial regulation of growth- and metabolism-related factors in RT zebrafish."; RL Zebrafish 10:237-248(2013). RN [5] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=24363414; RA Rocha F., Dias J., Engrola S., Gavaia P., Geurden I., Dinis M.T., RA Panserat S.; RT "Glucose overload in yolk has little effect on the long-term modulation of RT carbohydrate metabolic genes in zebrafish (Danio rerio)."; RL J. Exp. Biol. 217:1139-1149(2014). RN [6] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=24611545; RA Nolte H., Konzer A., Ruhs A., Jungblut B., Braun T., Kruger M.; RT "Global protein expression profiling of zebrafish organs based on in vivo RT incorporation of stable isotopes."; RL J. Proteome Res. 13:2162-2174(2014). RN [7] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=25609020; RA Rocha F., Dias J., Engrola S., Gavaia P., Geurden I., Dinis M.T., RA Panserat S.; RT "Glucose metabolism and gene expression in juvenile zebrafish (Danio rerio) RT challenged with a high carbohydrate diet: effects of an acute glucose RT stimulus during late embryonic life."; RL Br. J. Nutr. 113:403-413(2015). RN [8] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=29913146; RA Kuwabara S., Yamaki M., Yu H., Itoh M.; RT "Notch signaling regulates the expression of glycolysis-related genes in a RT context-dependent manner during embryonic development."; RL Biochem. Biophys. Res. Commun. 503:803-808(2018). RN [9] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=30218961; RA Zhao F., Wang H., Wei P., Jiang G., Wang W., Zhang X., Ru S.; RT "Impairment of bisphenol F on the glucose metabolism of zebrafish larvae."; RL Ecotoxicol. Environ. Saf. 165:386-392(2018). RN [10] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=30102881; RA Gong Y., Zhai G., Su J., Yang B., Jin J., Liu H., Yin Z., Xie S., Han D.; RT "Different roles of insulin receptor a and b in maintaining blood glucose RT homeostasis in zebrafish."; RL Gen. Comp. Endocrinol. 269:33-45(2018). RN [11] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=30448747; RA Wan Z., Wang C., Zhou J., Shen M., Wang X., Fu Z., Jin Y.; RT "Effects of polystyrene microplastics on the composition of the microbiome RT and metabolism in larval zebrafish."; RL Chemosphere 217:646-658(2019). RN [12] {ECO:0000313|RefSeq:NP_998417.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RX PubMed=30471337; RA Lin Y.S., Saputra F., Chen Y.C., Hu S.Y.; RT "Dietary administration of Bacillus amyloliquefaciens R8 reduces hepatic RT oxidative stress and enhances nutrient metabolism and immunity against RT Aeromonas hydrophila and Streptococcus agalactiae in zebrafish (Danio RT rerio)."; RL Fish Shellfish Immunol. 86:410-419(2019). RN [13] {ECO:0000313|RefSeq:NP_998417.1} RP IDENTIFICATION. RC STRAIN=AB {ECO:0000313|RefSeq:NP_998417.1}; RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+); CC Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00043797}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949; CC Evidence={ECO:0000256|ARBA:ARBA00043797}; 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:0000256|ARBA:ARBA00000435}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; CC Evidence={ECO:0000256|ARBA:ARBA00000435}; 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:0000256|ARBA:ARBA00000417}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; CC Evidence={ECO:0000256|ARBA:ARBA00000417}; 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:0000256|ARBA:ARBA00043834}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; CC Evidence={ECO:0000256|ARBA:ARBA00043834}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 1/4. CC {ECO:0000256|ARBA:ARBA00004888}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|ARBA:ARBA00005028}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004450}. CC -!- SIMILARITY: Belongs to the hexokinase family. CC {ECO:0000256|ARBA:ARBA00009225}. 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; BC048065; AAH48065.1; -; mRNA. DR RefSeq; NP_998417.1; NM_213252.1. DR GeneID; 406791; -. DR KEGG; dre:406791; -. DR AGR; ZFIN:ZDB-GENE-040426-2848; -. DR CTD; 3098; -. DR ZFIN; ZDB-GENE-040426-2848; hk1. DR OrthoDB; 5481886at2759; -. DR PhylomeDB; Q7ZUM3; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR Proteomes; UP000000437; Alternate scaffold 13. DR Proteomes; UP000000437; Chromosome 13. 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; IBA:GO_Central. DR GO; GO:0046835; P:carbohydrate phosphorylation; 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 GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 2. DR Gene3D; 3.30.420.40; -; 2. DR Gene3D; 3.40.367.20; -; 2. 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:SF10; HEXOKINASE-1; 1. DR Pfam; PF00349; Hexokinase_1; 2. DR Pfam; PF03727; Hexokinase_2; 2. DR PRINTS; PR00475; HEXOKINASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 4. DR PROSITE; PS00378; HEXOKINASE_1; 2. DR PROSITE; PS51748; HEXOKINASE_2; 2. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}; KW Immunity {ECO:0000256|ARBA:ARBA00022859}; KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198}; KW Innate immunity {ECO:0000256|ARBA:ARBA00022588}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAH48065.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q7ZUM3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 22..218 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 226..458 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT DOMAIN 470..667 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 674..907 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT COILED 463..494 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 918 AA; 102828 MW; 09E759B881F5DFAA CRC64; MIAAQLLAYY FTELKDDQVK KIDKYLYAMR FSDETLRDIM ARFRREMENG LARDTNPTAT AKMLPTFVRS IPDGSEKGDF IALDLGGSNF RILRVKVSHE KKQTVQMESQ IYETPEDIIH GSRSRLFDHV AECLGDFMEK QKIKDKKLPV GFTFSFPCSQ SKLDEAVLLT WTKRFKVNGV EGMDVVKLLN KAIKKRGDYE ADIMAVVNDT VGTMMTCGFD DQRCEVGIII GTGTNACYME ELRHMDMVEG DEGRMCINTE WGAFGDDGTL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM YMGELVRLIL VKMAKEGLLF EGRITPELLT KGKIETKHVS AIEKSKEGLT KAKEILTRLG VEPSEDDCIA VQHVCAIVSF RSANLIAATL GAILTRLKDN KNTPRLRTTV GIDGSLYKMH PQYARRLHKT VRRLVPESDV RFLLSESGSG KGAALVTAWA YRLADQERQI AETLEEFRLT KDQLLEVKKR MRTEIQNGLS KSTQNTATVK MLPTYVRSTP DGSENGDFLA LDLGGTNFRV LLVKIRSGKR RTVEMHNKIY AIPIEVMQGT GEELFDHIVY CISDFLDYMG MKNARLPLGF TFSFPCRQTS LDAGLLVNWT KGFKATDCEG EDVVGLLREG IKRREEFDLD VVAIVNDTVG TMMTCAYEEP TCEVGLIAGT GSNACYMEEM RNIETVSGEE GRMCVNMEWG AFGDNGCLDD IRTKYDDAVD DLSLNAGKQK YEKMCSGMYL GEIVRNILID LTKRGFLFRG QISETLKTRG IFETKFLSQI ESDRLALLQV RSILQHLGLD STCDDSIIVK EVCGAVSRRA AQLCGAGMAA VVDKIRENRG LDHLDITVGV DGTLYKLHPH FSRIMHQTVK ELAPKCNVTF LLSEDGSGKG AALITAVGCR LRQQEQKS //