GenomeNet

Database: UniProt
Entry: A0A2G8SKI7_9APHY
LinkDB: A0A2G8SKI7_9APHY
Original site: A0A2G8SKI7_9APHY 
ID   A0A2G8SKI7_9APHY        Unreviewed;       496 AA.
AC   A0A2G8SKI7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=GSI_03047 {ECO:0000313|EMBL:PIL34272.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL34272.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL34272.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL34272.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIL34272.1}.
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; AYKW01000005; PIL34272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8SKI7; -.
DR   STRING; 1077348.A0A2G8SKI7; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000230002; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
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:UP000230002};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          43..239
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          245..483
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   496 AA;  55067 MW;  32B8AD30BFF253CF CRC64;
     MSSRRGSSTV LHPSGQTVTT FTKHSADDDV LPHATKKTMA DHLRKYEALF NLTPQRMRMI
     VEAFKESLEL GLSKHGQIVP MIPTYVFGWP TSQELGNFLA VDLGGTNLRV CLVTLEGKGK
     FEITQAKYRL SEEQKQDEGQ KLFDFCGECL KAFVDANHES GLIPKGSVLP LGFTFSYPCA
     QDRIDHGVLI RWTKGFGAPN TEGHDVVEMF RNSLSKHQVP AEIVALTCDT TGTLIASHYV
     NPKTRIACIF GTGCNAAYME KVQDIPKIAN LGIDPEMQMA INCEWGAFDS FEHENLPRTK
     YDQTIDESSN KPGEQAFEKL ISGRYLGEIL RLIICELIDE GVLFLGQNTY KIEIAYSLDT
     AFLSLMESDP TDELLMIIGI FNHFFALETT LAERQFFRAL AKLVGRRAAR LSACGIAAIV
     SRMGYLDEGC AVGADGSLYN KYPMFPERIH EGLFDIFGEK GKNVVTYRAE DGSGIGSAIV
     AAMTKFRKEA QIYPNL
//
DBGET integrated database retrieval system