ID   A4J5I2_DESRM            Unreviewed;       440 AA.
AC   A4J5I2;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Hexokinase {ECO:0000313|EMBL:ABO50335.1};
DE            EC=2.7.1.1 {ECO:0000313|EMBL:ABO50335.1};
GN   OrderedLocusNames=Dred_1810 {ECO:0000313|EMBL:ABO50335.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50335.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO50335.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO50335.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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. {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; CP000612; ABO50335.1; -; Genomic_DNA.
DR   RefSeq; WP_011878147.1; NC_009253.1.
DR   AlphaFoldDB; A4J5I2; -.
DR   SMR; A4J5I2; -.
DR   STRING; 349161.Dred_1810; -.
DR   KEGG; drm:Dred_1810; -.
DR   eggNOG; COG5026; Bacteria.
DR   HOGENOM; CLU_014393_5_3_9; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000001556; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABO50335.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABO50335.1}.
FT   DOMAIN          8..202
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          209..430
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   440 AA;  48589 MW;  DDEF4BB9FF896CFE CRC64;
     MGRLARKLNQ IEKDFYLSLG MVNDIARNFR AEMVAGQSGD SSLKMLHTFI TPPTGQETGE
     FLAVDFGGTN VRIQLVELLG KGRYRIRKNH SVMLCDPAGS YDYTLECTSG EELFDFIVEQ
     IVKLIDNKTH YFLGHTFSFP TKQIDPARAI LINWTKEFKT AGTEGKEVTS LLENALKRKS
     IRNVQPLSII NDTTATLLTA AYGNDCANIG SICGTGHNTC YLEAAAGPVI INMESGNFNK
     FPLTTFDLVL NEASEQPNLQ QLEKAVSGRY VGEIVRLIIL DFVAEKMLFS RGINGIDEPF
     SIQAPEVSLM IRGNHKPDDL LDLAHWVGVK WCVKSPSADE LIALRCIAQT VICRASRLIA
     ATFLGVLQHI DPELKSRQVI GIDGSMFQNM PFFLQGILEI FSNIYEDKAA NIVLKYIRDA
     SGVGAAIAAA RMKSLQVKGN
//