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Database: UniProt
Entry: A0A075ANT2_ROZAC
LinkDB: A0A075ANT2_ROZAC
Original site: A0A075ANT2_ROZAC 
ID   A0A075ANT2_ROZAC        Unreviewed;       480 AA.
AC   A0A075ANT2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=O9G_000055 {ECO:0000313|EMBL:EPZ31577.1};
OS   Rozella allomycis (strain CSF55).
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Rozella.
OX   NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ31577.1, ECO:0000313|Proteomes:UP000030755};
RN   [1] {ECO:0000313|EMBL:EPZ31577.1, ECO:0000313|Proteomes:UP000030755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSF55 {ECO:0000313|EMBL:EPZ31577.1,
RC   ECO:0000313|Proteomes:UP000030755};
RX   PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA   James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA   Stajich J.E.;
RT   "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT   microsporidia.";
RL   Curr. Biol. 23:1548-1553(2013).
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}.
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DR   EMBL; KE561209; EPZ31577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075ANT2; -.
DR   STRING; 988480.A0A075ANT2; -.
DR   EnsemblFungi; EPZ31577; EPZ31577; O9G_000055.
DR   HOGENOM; CLU_014393_5_1_1; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000030755; 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; 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: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; 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:UP000030755};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          40..232
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          253..478
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   480 AA;  53351 MW;  D6BFCBDFE2F11427 CRC64;
     MRSNVTTFLI GAILGAGLRD LLRNLSLNYK GDDEEPIYVE LESQFILSPD ILYAILKKFT
     ECMSNGLAEE NYKDMPMIPS FVERLPKGNE TGYFLAIDLG GTNARICLVD LKGTREQPVL
     IQKKAVVPDD VKAGKSEDLF NWLADLTFEF VNENEITNEE KIKLGFTFSF PVVQSGLSKG
     KLTQWAKGFS CEGVVGKDVV EPLQKALHNK GLEIEVVALV NDTVGTLVSH SYVDEMTFMG
     VILGILILNV SKGTGTNAAY VEECSRIKKK DLKGKQMVIN TEWGAFDSER KYLPYTKYDN
     HLNKESLYPN QQNFEKMISG MYLGEITRHV LVDLHARGLL FPASNINCLL KRESFLTSQM
     SRIERDNSKN LDDVKIVLEK NIGISETDLN DRKLVKHVCK CVGTRAAQLS AMAIGAVLKH
     SGRWDCTVAI DGSLFEHYPN FKLRIQQTLR QLFGVVSDDV KLSLANDGSG IGAALIAASC
//
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