ID G1MFD2_AILME Unreviewed; 917 AA. AC G1MFD2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Hexokinase-2 {ECO:0000256|ARBA:ARBA00039453}; DE EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324}; DE AltName: Full=Hexokinase type II {ECO:0000256|ARBA:ARBA00041371}; GN Name=HK2 {ECO:0000313|Ensembl:ENSAMEP00000018062.1}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000018062.1, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000018062.1, ECO:0000313|Proteomes:UP000008912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J., RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., RA Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000018062.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|ARBA:ARBA00001397}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; CC Evidence={ECO:0000256|ARBA:ARBA00001397}; 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 -!- 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 RefSeq; XP_002921507.1; XM_002921461.3. DR AlphaFoldDB; G1MFD2; -. DR STRING; 9646.ENSAMEP00000018062; -. DR Ensembl; ENSAMET00000018793.2; ENSAMEP00000018062.1; ENSAMEG00000017077.2. DR GeneID; 100470774; -. DR KEGG; aml:100470774; -. DR CTD; 3099; -. DR eggNOG; KOG1369; Eukaryota. DR GeneTree; ENSGT00950000182787; -. DR HOGENOM; CLU_014393_1_0_1; -. DR InParanoid; G1MFD2; -. DR OMA; SYLVSWT; -. DR OrthoDB; 5481886at2759; -. DR TreeFam; TF314238; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004340; F:glucokinase activity; IEA:Ensembl. DR GO; GO:0005536; F:glucose binding; IEA:InterPro. DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; IEA:Ensembl. DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro. DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; IEA:Ensembl. DR GO; GO:0035795; P:negative regulation of mitochondrial membrane permeability; IEA:Ensembl. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IEA:Ensembl. DR GO; GO:0046324; P:regulation of glucose import; IEA:Ensembl. 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:SF4; HEXOKINASE-2; 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 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 22..219 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 225..459 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT DOMAIN 471..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" SQ SEQUENCE 917 AA; 102485 MW; DA0431CD20CE5F49 CRC64; MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDENLLEIS KRFRKEMEKG LGATTHPTAS VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLRVRVTDN GLQKVEMENQ IYAIPEDLMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCVQ TKLDESFLVS WTKGFKSSGV EGKDVVTLIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DQNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGTL DDFRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKVSPGLLT TGQFETKDVS DIEGEKDGTR KAREVLLRLG MDPTQEDCVA THRICQIVST RSASLCAATL AAVLRRIKEN KGEERLRSTI GVDGSVYKKH PHFAKRLHKA VRRLVPDCDV RFLRSEDGSG KGAAMVTAVA YRLADQHRAR QNTLESLKLS REQLLEVKRR MNVEMERGLS KETHAIAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV LLVRVRNGKR RGVEMHNKIY SIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVMLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGYEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGRQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILRHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDKIRENRG LDTLKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LESEDGSGKG AALITAVACR IREAGQR //