ID B2AR43_PODAN Unreviewed; 186 AA. AC B2AR43; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN ORFNames=PODANS_4_8700 {ECO:0000313|EMBL:CAP66621.1}; OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OS (Pleurage anserina). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora; OC Podospora anserina. OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP66621.1}; RN [1] {ECO:0000313|EMBL:CAP66621.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP66621.1}; RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77; RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M., RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V., RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M., RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D., RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B., RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H., RA Debuchy R., Wincker P., Weissenbach J., Silar P.; RT "The genome sequence of the model ascomycete fungus Podospora anserina."; RL Genome Biol. 9:R77.1-R77.22(2008). RN [2] {ECO:0000313|EMBL:CAP66621.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP66621.1}; RA Genoscope - CEA; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. 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; CU633895; CAP66621.1; -; Genomic_DNA. DR RefSeq; XP_001905955.1; XM_001905920.1. DR AlphaFoldDB; B2AR43; -. DR GeneID; 6190085; -. DR KEGG; pan:PODANSg2983; -. DR VEuPathDB; FungiDB:PODANS_4_8700; -. DR HOGENOM; CLU_1454998_0_0_1; -. DR OrthoDB; 5481886at2759; -. DR UniPathway; UPA00109; UER00180. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005536; F:glucose binding; IEA:InterPro. DR GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro. 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; IPR022673; Hexokinase_C. DR InterPro; IPR022672; Hexokinase_N. DR PANTHER; PTHR19443; HEXOKINASE; 1. DR PANTHER; PTHR19443:SF24; HEXOKINASE YLR446W-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; PS51748; HEXOKINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007}; KW Glycolysis {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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 1..49 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 57..178 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" SQ SEQUENCE 186 AA; 19705 MW; 129A9A1D1B20B1FB CRC64; MGKSFHAADG LLNQNLSSIL QTSCLHHNLH VSLSAIVNDS SATLLSAAYS HPSTTTFGLI LGTGVNIAAY LPVTTISPSK LPPRPQTLAT HVVVNTELGM FGGPSLPSTK WDKTLKASHP RPDFQPLEHL VSGFYLGEVA RLILVDAIHE TGAFGGVVPD SLAREYTLDA KTLSLLERCS PSAVPL //