ID A7EJB4_SCLS1 Unreviewed; 554 AA. AC A7EJB4; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 03-MAY-2023, entry version 82. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN ORFNames=SS1G_05407 {ECO:0000313|EMBL:EDO02930.1}; OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) OS (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO02930.1, ECO:0000313|Proteomes:UP000001312}; RN [1] {ECO:0000313|Proteomes:UP000001312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312}; RX PubMed=21876677; DOI=.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). 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 -!- 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; CH476626; EDO02930.1; -; Genomic_DNA. DR RefSeq; XP_001593979.1; XM_001593929.1. DR AlphaFoldDB; A7EJB4; -. DR STRING; 665079.A7EJB4; -. DR EnsemblFungi; EDO02930; EDO02930; SS1G_05407. DR GeneID; 5490348; -. DR KEGG; ssl:SS1G_05407; -. DR VEuPathDB; FungiDB:sscle_08g066530; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_0_1; -. DR InParanoid; A7EJB4; -. DR OMA; YPNFEGY; -. DR OrthoDB; 5481886at2759; -. DR UniPathway; UPA00109; UER00180. DR Proteomes; UP000001312; 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:0019158; F:mannokinase activity; IEA:EnsemblFungi. 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:0019660; P:glycolytic fermentation; IEA:EnsemblFungi. 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; 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:SF30; GLUCOKINASE-1-RELATED; 1. DR PANTHER; PTHR19443; HEXOKINASE; 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:UP000001312}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 8..219 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 229..531 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" SQ SEQUENCE 554 AA; 60195 MW; 333041BC5A3EB406 CRC64; MSLLAESKRV AAEFEYSDED VRRGVAEFIA EMNEGLEKNA TNMSQIPTYV TGVPNGTEKG LYLAVDLGGT NFRVCSIQLH GDTTFSLTQS KVAIPRELML AKTASDLFSF LAKQIELFLK THHEDHFAAH IRRRNTVSTP EGFRDEHIFR LGFTFSFPVH QIGINRGTLI RWTKGFDIAD AVGQDVCELL QKEIDKLHLP VKVAALVNDT VGTLMARAYT SPGKAQTVLG AIFGTGTNGA YVEKLEKLTK PMEGDFDKTT GEMVVNTEWG SFDNGLKVLP NTIYDQILDK DSVNPGIQMF EKRVSGMFLG EILRTTLIEM MKSPISTLFK DKSSADNDYR STTNIDENGA LFKQWAVDSS ILSIAEADNS IGLRALRQEL EKSLGVSAAS LEDAQTVKEI AHAIGKRAAR LAAVAIGAVV LHTGRLDNIS DANKPKSTTS IVQDVQDLKL ADAASATASK LADTAGLKIN EEDIIDIGVD GSLVEFYPGF EEYMREALRA MDGIGAAGER RIRIGIAKDG SGVGAALIAL VAAGMEKQQD YIGDLRSKYG AIAE //