ID A0A165ENH8_9APHY Unreviewed; 546 AA.
AC A0A165ENH8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=LAESUDRAFT_736395 {ECO:0000313|EMBL:KZT07433.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07433.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07433.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07433.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427619; KZT07433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ENH8; -.
DR STRING; 1314785.A0A165ENH8; -.
DR InParanoid; A0A165ENH8; -.
DR OrthoDB; 5481886at2759; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000076871; Unassembled WGS sequence.
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: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; 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 Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 150..254
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 265..539
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 546 AA; 59574 MW; 60F4C2F997F79DA2 CRC64;
MVGSTPNPTP VRTNGLGAYD FAINEGKEIQ FTITVAESYP TVTEIYCGVV NGQVILNTLR
RWSSVTSHFY VVTRRQHLAL AQAAARNRAH QPADIPSRPL GRLWDEWKVE CGGERLRVVK
GRENEDLMVA TPEPQRSGDA GPYDGHYYLT DSVDTFLTEF SSAVSSPTTA DITNPFESSA
PLSIPLGLTF SFPVEQTVID GGKILTWTKG FSAKNALGKD IVSLLQDAFD RKHLHVHCVV
LVNDTVGTLL SRAYAAESCL LERCAIFGTG TNSADVENVE NITKLGNSPA RQKGGLMIIN
AEWSTFNNTH TSLPTASYDN KLDQDSINPR KQAFKKFISG MYLGEITRNI LLSFIDAMLK
PLLFNGNSSE PLNTHYGLNT AVMSEVESTW ELGRTDAAKV NSANGHVPNW QSIHFTDAKA
LGKDDIAWLE CIRKIVIQRL QVLDLENMSL RDAVIVRLSR TAVTVVLMQT GNAKLRGGVQ
ALKENLIIGV DGSLIQHYPN FEAQLHSSLQ SLAGEAVEKC VEIDLAKDGS GAGATLCALQ
AIKQGL
//
