ID Q753N3_EREGS Unreviewed; 488 AA. AC Q753N3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 114. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN ORFNames=AGOS_AFR279C {ECO:0000313|EMBL:AAS53650.1}; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS53650.1, ECO:0000313|Proteomes:UP000000591}; RN [1] {ECO:0000313|EMBL:AAS53650.1, ECO:0000313|Proteomes:UP000000591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] {ECO:0000313|Proteomes:UP000000591} RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). 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 -!- 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 -!- SIMILARITY: Belongs to the hexokinase family. CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}. 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; AE016819; AAS53650.1; -; Genomic_DNA. DR RefSeq; NP_985826.1; NM_211181.1. DR AlphaFoldDB; Q753N3; -. DR STRING; 284811.Q753N3; -. DR EnsemblFungi; AAS53650; AAS53650; AGOS_AFR279C. DR GeneID; 4622089; -. DR KEGG; ago:AGOS_AFR279C; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_2_1; -. DR InParanoid; Q753N3; -. DR OMA; ADCVQQF; -. DR OrthoDB; 5481886at2759; -. DR UniPathway; UPA00109; UER00180. DR Proteomes; UP000000591; Chromosome VI. 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-UniRule. 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 GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 1.10.287.1250; -; 1. DR Gene3D; 3.30.420.40; -; 1. DR Gene3D; 3.40.367.20; -; 1. 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:SF16; HEXOKINASE TYPE 1-RELATED; 1. DR Pfam; PF00349; Hexokinase_1; 1. DR Pfam; PF03727; Hexokinase_2; 1. DR PRINTS; PR00475; HEXOKINASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00378; HEXOKINASE_1; 1. DR PROSITE; PS51748; HEXOKINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU362007}; KW Reference proteome {ECO:0000313|Proteomes:UP000000591}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 27..221 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 227..470 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" SQ SEQUENCE 488 AA; 53995 MW; 57FF619EF09D2A5A CRC64; MVHLGPKKPP TRKGSMADVP KTLVEQIASF ERIFTVSAEK LQEITKHFVT ELDKGLSKKG GNIPMIPGWV MDYPTGNETG DYLAIDLGGT NLRVVLVKLL GNHQFDTTQS KYRLPNRMRT TQNASELWDF IAESLKDFLE EQFPEGVHQT LPLGFTFSYP ASQDKINMGI LQRWTKGFDI PGVEGHDVVP MLQESLRKVN VPIEVVALIN DTTGTLVASL YTDAETKMGV IFGTGVNGAY YDVVKDIEKL EGRLPEDIPP ESAMAINCEY GSFDNEHLVL PRTKYDILID EQSPRPGQQA FEKMTSGYYL GEVLRLALLD LHGQGLIFQG QDISKLETPY VMDTSFPARI EDDPFENLEE TDDLFKDNLD IDTTRPERKL IRKLSEMIGN RAARLSVCGI AAICQKRGYE TAHIAADGSV FNKYPGFQTR AAEGLRDIYG WEHSSSQDYP IKIVAAEDGS GAGAAVIAAL TTKRLAAGKS VGLPEAQN //