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Database: UniProt
Entry: A0A132A2T7_SARSC
LinkDB: A0A132A2T7_SARSC
Original site: A0A132A2T7_SARSC 
ID   A0A132A2T7_SARSC        Unreviewed;       308 AA.
AC   A0A132A2T7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=QR98_0037780 {ECO:0000313|EMBL:KPM05317.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM05317.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM05317.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM05317.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000435};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000256|ARBA:ARBA00000435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000417};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000256|ARBA:ARBA00000417};
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:KPM05317.1}.
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DR   EMBL; JXLN01010207; KPM05317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A132A2T7; -.
DR   VEuPathDB; VectorBase:SSCA001182; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000616769; 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:0019318; P:hexose metabolic 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          29..212
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          219..295
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   308 AA;  35108 MW;  C272EB5AC9F0D867 CRC64;
     MEDHREFYYD NDEYFNPKLN LNDSVLKEKR IINAIDSVLS NKDSSKNSEF LPLFNTLVTK
     YPNNQESGVF LGLDIGGTNL RIVLLNLKDS DESDRKIIID NYDVPVEFRQ STSEKFFDYL
     AGCLKNFYDK NQNILKDSPS RIPLGFSFSF CFEQLTINSG RCLQFSIATN LIDGIGKCPV
     QLFQKSIDSL QLPVEIVALA NDSTTTLICG KYFDPKTEIS LILGSGGNVA YVENVAADFR
     IENPREKFGL PLAPEKMIIN SEVFLFGDNH QIDDLKTCYD FELDAMSLLP GNYTYVSRYR
     LPLYFLNR
//
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