ID   GAL1_STRLI              Reviewed;         397 AA.
AC   P13227;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 113.
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};
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3335481; DOI=10.1128/jb.170.1.203-212.1988;
RA   Adams C.W., Fornwald J.A., Schmidt F.J., Rosenberg M., Brawner M.E.;
RT   "Gene organization and structure of the Streptomyces lividans gal operon.";
RL   J. Bacteriol. 170:203-212(1988).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RA   Gibson T.J.;
RL   Unpublished observations (MAR-1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26748.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M18953; AAA26748.1; ALT_FRAME; Genomic_DNA.
DR   PIR; C28669; KISMG.
DR   AlphaFoldDB; P13227; -.
DR   SMR; P13227; -.
DR   UniPathway; UPA00214; -.
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..397
FT                   /note="Galactokinase"
FT                   /id="PRO_0000184626"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         36..39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
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         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   SITE            30
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
SQ   SEQUENCE   397 AA;  41984 MW;  337D8007B5BD0619 CRC64;
     MGEAVGEPSA SGSGSCTGRS RRGCGRRAGR ENLIGEHTDY NDGFVMPSAL PHQVAAVSRR
     ERRILRLHSA DVDADPVELR VADLAPASDK SWTAYPSGVL WALREAGHEL TGADVHLAST
     VPSGAGLSSS AALEVRPLAM NDLYALALRG WQLARLCQRA ENVYVGAPVG IMDQTASACC
     RGGHALFLDT RDLSQRQIPF DLAAEGMRLL VVDTRVKHSH SEGEYGKRRA GCEKGAALLG
     VDALCDVPYA DLDAALERLG DEEEVRRLVR HVVTEDERVE RVVALLESGD TRRIGAVLVE
     GHASLRDDFR ISCPELDLVV DTALASAALG RRMTGGGFGG SAIVLVEAAA VDAVTKAVED
     AFAAAGLKRP RVFEAVPRRG AAPGLTVSRA ASPACTP