ID   D4ALA3_ARTBC            Unreviewed;       581 AA.
AC   D4ALA3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=ARB_05100 {ECO:0000313|EMBL:EFE36162.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE36162.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE36162.1}.
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; ABSU01000002; EFE36162.1; -; Genomic_DNA.
DR   RefSeq; XP_003016807.1; XM_003016761.1.
DR   AlphaFoldDB; D4ALA3; -.
DR   STRING; 663331.D4ALA3; -.
DR   GeneID; 9526284; -.
DR   KEGG; abe:ARB_05100; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_4_1_1; -.
DR   OMA; FPVEQTS; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000008866; 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   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; 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   Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          86..267
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          273..573
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   REGION          34..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  62080 MW;  8F1CAE1D83637357 CRC64;
     MGKGTLEQVA LRLRQLFDSL LSVLQRLLRL SQKQKTTATT ATTPSKTPSK TCEKRPSSLR
     CRRSLDDLAA DVQRQFTSHL STARLAAMAA GIRLQLDRCA KSSPVCMLPS FNHALPSGCE
     RGTFLALDVG GSTFRVALVE LAGHGAMHIR RIASSAIDEP VKLLEGRAFF DWIALRILDM
     LRAGDEGYGR DSSSPLPMGL SWSFPIDQTS IRSGLVLSMG KGFLCSNGTV GEDLGDLIMA
     ACRKHQLNVR IEAIVNDSSA TLLSRAYIDP STRMSLILGT GTNVAIHYPT RAIGREKFGD
     RPAAWFDKAS HVIINTEMSM FGGGGVLPMT RWDDDLNRAH IKPDYQPLEY LVTGRYIGEI
     VRLIVVEAVA VAGLFAGELP ASLRLPYSLD TAIVACIEAD TSSTLDKSAA MLTASHAFAV
     APSTADMQFL QTVCKCVSRR GAAYLATAIY SLWRLSNESE SPASSSPEHT RDDLLLTKGL
     STTADLEIGQ AVTIACDGTV INKYPGFRST CQAYLNSLTS HANSNSNSSS NSTADSADSG
     SDSATETESD KPMISLDPAP ESGIFGAAVA VAVALPSSPS S
//