ID D8SWF6_SELML Unreviewed; 484 AA. AC D8SWF6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 63. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN ORFNames=SELMODRAFT_269299 {ECO:0000313|EMBL:EFJ11217.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ11217.1, ECO:0000313|Proteomes:UP000001514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I., RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). 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; GL377648; EFJ11217.1; -; Genomic_DNA. DR RefSeq; XP_002987642.1; XM_002987596.1. DR AlphaFoldDB; D8SWF6; -. DR STRING; 88036.D8SWF6; -. DR EnsemblPlants; EFJ11217; EFJ11217; SELMODRAFT_269299. DR Gramene; EFJ11217; EFJ11217; SELMODRAFT_269299. DR KEGG; smo:SELMODRAFT_269299; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_1_1; -. DR InParanoid; D8SWF6; -. DR OMA; RTIYEFM; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR Proteomes; UP000001514; Unassembled WGS sequence. 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: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; 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:UP000001514}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 29..227 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 234..470 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 484 AA; 53454 MW; 1CF81916AFF13F80 CRC64; MGSDRSKSSK NKPRKMIPKG LEAAHSMRDK FRNACATPVE TLRKISQDML SQMEAGLQSD GESRLRMLLS FVEHLPCGNE TGLFYGLDLG GTNFRVLRVQ LGGKEKRILK QESKVDSIPS EIMTSTNEEL FDYIARVLAD FVATEGVDCN LILGQKRELG FTFSFPVSQE SLNSGKLVKW TKGFAIAETI GQDVVKELQA AMERCKLDMH VIAMVNDTTG TLAGGRYWNE DVMAGLILGT GSNACYVEQT SEIPKWPPSL PKPEETVINI EWGHFWSPHI PKTEIDDDLD AESVHPGQQV FEKLFSGMYL GDIVRRMILK LAEQACLLGG VTEIPSNMAT PFVLRTRDVS IMHEDESENL ENVARVMETI FGLKELPLEV RKVIKDVCEI TAARGARLVA AGIVGIVRKI GGRKKKICIA IDGSLYEHYT KFRAKLHEAL VELLGQEAAA KVVIELSKDG SGLGAALLAA SHSKKDLEDK CDKQ //