ID   GAL1_SALDC              Reviewed;         382 AA.
AC   B5FP41;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Galactokinase {ECO:0000255|HAMAP-Rule:MF_00246};
DE            EC=2.7.1.6 {ECO:0000255|HAMAP-Rule:MF_00246};
DE   AltName: Full=Galactose kinase {ECO:0000255|HAMAP-Rule:MF_00246};
GN   Name=galK {ECO:0000255|HAMAP-Rule:MF_00246}; OrderedLocusNames=SeD_A0869;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D-
CC       galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
CC       {ECO:0000255|HAMAP-Rule:MF_00246}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate
CC         + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00246};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00246}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00246}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00246}.
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DR   EMBL; CP001144; ACH77684.1; -; Genomic_DNA.
DR   RefSeq; WP_001049364.1; NC_011205.1.
DR   AlphaFoldDB; B5FP41; -.
DR   SMR; B5FP41; -.
DR   KEGG; sed:SeD_A0869; -.
DR   HOGENOM; CLU_017814_2_1_6; -.
DR   OMA; PVCYNLR; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000008322; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004335; F:galactokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00246; Galactokinase; 1.
DR   InterPro; IPR000705; Galactokinase.
DR   InterPro; IPR022963; Galactokinase_bac.
DR   InterPro; IPR019741; Galactokinase_CS.
DR   InterPro; IPR019539; GalKase_N.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006206; Mevalonate/galactokinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1.
DR   Pfam; PF10509; GalKase_gal_bdg; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000530; Galactokinase; 1.
DR   PRINTS; PR00473; GALCTOKINASE.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00131; gal_kin; 1.
DR   PROSITE; PS00106; GALACTOKINASE; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..382
FT                   /note="Galactokinase"
FT                   /id="PRO_1000100839"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         34..37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   SITE            28
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
SQ   SEQUENCE   382 AA;  41246 MW;  764243641DAC1EBC CRC64;
     MNLKEKTRAL FAEIFGYPAT HTIQAPGRVN LIGEHTDYND GFVLPCAIDY QTVISCAPRD
     DRTVRVIAAD YDNQVDEFSL DAPIVTHDSQ QWSNYVRGVV KHLQQRNNAF GGVDMVISGN
     VPQGAGLSSS ASLEVAVGTV FQQLYHLPLD GAQIALNGQE AENQFVGCNC GIMDQLISAL
     GKKDHALLID CRTLGAKAVS MPKGVAVVII NSNFKRTLVG SEYNTRREQC ETGARFFQQP
     ALRDVSLEAF NAVASELDPV VAKRVRHVLS ENARTVEAAS ALEKGDLQRM GQLMAESHAS
     MRDDFEITVP QIDTLVDIVK ATIGDQGGVR MTGGGFGGCV VALIPEDLVP AVQQAVAQQY
     EAKTGIKETF YVCKPSQGAG QC