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Database: UniProt
Entry: A0A1J4MKA1_9CRYT
LinkDB: A0A1J4MKA1_9CRYT
Original site: A0A1J4MKA1_9CRYT 
ID   A0A1J4MKA1_9CRYT        Unreviewed;       532 AA.
AC   A0A1J4MKA1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=cubi_02509 {ECO:0000313|EMBL:OII73277.1};
OS   Cryptosporidium ubiquitum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=857276 {ECO:0000313|EMBL:OII73277.1, ECO:0000313|Proteomes:UP000186176};
RN   [1] {ECO:0000313|EMBL:OII73277.1, ECO:0000313|Proteomes:UP000186176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=39726 {ECO:0000313|EMBL:OII73277.1};
RA   Liu S., Roellig D.M., Guo Y., Li N., Frace M.A., Tang K., Zhang L.,
RA   Feng Y., Xiao L.;
RT   "Reductive evolution of mitochondrial metabolism and differential evolution
RT   of invasion-related proteins in Cryptosporidium.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OII73277.1}.
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DR   EMBL; LRBP01000017; OII73277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4MKA1; -.
DR   VEuPathDB; CryptoDB:cubi_02509; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000186176; 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   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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          14..253
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          290..526
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   532 AA;  59917 MW;  488E817C275925B4 CRC64;
     MEEENQTKEL FDLYEKYFFL PKSRLMELVD DFCISLEDGL KNHTNPLKIN KCYSNYKPFK
     MLDSCIDKLP TGKEKGVYYA IDMGGTNLRC VRVNLLGNGQ SETKFKKTKL TEMKVFASEK
     VLNGSKCSKI CQKEVNILDK TVSSETMFNS IASFFNEFLK ECGDLNDLGS ININSFPIEV
     AFTFSFPTMQ FGIANANLLI WTKGIETGRS TNDPVEGKDI GDQLNSAFKR NGIPACCKCI
     VNDTVGTLLS AMYDLNVNNC NINNHFSKVN ENISKEVNTL TRKSENKPLV GIVVGTGVNA
     CYYEPDSLNF GYKGVIINTE CGDFYSSKLP STDCDLTIDW FSDNRGKQRF EKMISGTYLG
     EISRLLIINF LKYKTPKIFF KKDSFKTEHI AEIISQFNDS YHNFNQNHDS SCNQNLKSIE
     NYLRETFSSD FDHNSTHIIA RISQMVLMRA ASLVSVLLAA FIKRINKSHN EVIIAIDGSV
     WTKIPTFQNY VKKSLSSIIQ ESGNLGSIYF YESDDGSGRG AAVLASTISH IH
//
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