ID   E1WP67_BACF6            Unreviewed;       402 AA.
AC   E1WP67;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative hexokinase {ECO:0000313|EMBL:CBW23022.1};
GN   OrderedLocusNames=BF638R_2514 {ECO:0000313|EMBL:CBW23022.1};
OS   Bacteroides fragilis (strain 638R).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW23022.1, ECO:0000313|Proteomes:UP000008560};
RN   [1] {ECO:0000313|EMBL:CBW23022.1, ECO:0000313|Proteomes:UP000008560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638R {ECO:0000313|EMBL:CBW23022.1,
RC   ECO:0000313|Proteomes:UP000008560};
RX   PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA   Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA   Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA   Barron A., Clark L., Bentley S.D., Parkhill J.;
RT   "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT   strain capsule diversity in three strains of Bacteroides fragilis.";
RL   Microbiology 156:3255-3269(2010).
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. {ECO:0000256|ARBA:ARBA00004921}.
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000256|ARBA:ARBA00005007}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225}.
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DR   EMBL; FQ312004; CBW23022.1; -; Genomic_DNA.
DR   RefSeq; WP_014298972.1; NC_016776.1.
DR   AlphaFoldDB; E1WP67; -.
DR   SMR; E1WP67; -.
DR   KEGG; bfg:BF638R_2514; -.
DR   PATRIC; fig|862962.3.peg.2573; -.
DR   HOGENOM; CLU_014393_5_3_10; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000008560; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; 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; -; 2.
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; 2.
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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBW23022.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..185
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          196..277
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   DOMAIN          302..401
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   402 AA;  45175 MW;  5D11AB07C0CCBE7C CRC64;
     MEKNIFKLDN EQLKGIAHAF REKVEEGLNK NNAEIQCIPT FILPKATDIK GKALVLDLGG
     TNYRVAIVDF STEKPIIYPN NGWKKDMSIM KSPGYTREEL FKELADLIVE IKREEEMPIG
     YCFSYPTESI PGGDARLLRW TKGVDIREMV GQFVGKPLLD YLNEKNKIRF TGVKVLNDTI
     ASLFAGLTDK SYDAYIGLIV GTGTNMATFI PSDKITKLDP ECHVQGLIPV NLESGNFYPP
     FLTAVDDTVD ATSDSLGKQR FEKAVSGMYL GDILKAAFPL EEFEEKFDAR KLTAIMNYPD
     IHKDIYVQVA HWIYNRSAQL VAASLAGLIA LLKSYNRDIH RVCLIAEGSL FWSESRKDKN
     YNILVMEKLQ ELLRELELED VEVHINSMDN ANLIGTGIAA LS
//