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Database: UniProt
Entry: A0A0R1U9F6_9LACO
LinkDB: A0A0R1U9F6_9LACO
Original site: A0A0R1U9F6_9LACO 
ID   A0A0R1U9F6_9LACO        Unreviewed;       387 AA.
AC   A0A0R1U9F6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Galactokinase {ECO:0000256|ARBA:ARBA00012315, ECO:0000256|HAMAP-Rule:MF_00246};
DE            EC=2.7.1.6 {ECO:0000256|ARBA:ARBA00012315, ECO:0000256|HAMAP-Rule:MF_00246};
DE   AltName: Full=Galactose kinase {ECO:0000256|ARBA:ARBA00029590, ECO:0000256|HAMAP-Rule:MF_00246};
GN   Name=galK {ECO:0000256|HAMAP-Rule:MF_00246};
GN   ORFNames=FC46_GL000455 {ECO:0000313|EMBL:KRL89958.1};
OS   Lactobacillus kalixensis DSM 16043.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423763 {ECO:0000313|EMBL:KRL89958.1, ECO:0000313|Proteomes:UP000051036};
RN   [1] {ECO:0000313|EMBL:KRL89958.1, ECO:0000313|Proteomes:UP000051036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16043 {ECO:0000313|EMBL:KRL89958.1,
RC   ECO:0000313|Proteomes:UP000051036};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_00246};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|HAMAP-Rule:MF_00246}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00246}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000256|ARBA:ARBA00006566, ECO:0000256|HAMAP-Rule:MF_00246}.
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:KRL89958.1}.
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DR   EMBL; AZFM01000016; KRL89958.1; -; Genomic_DNA.
DR   RefSeq; WP_057798755.1; NZ_AZFM01000016.1.
DR   AlphaFoldDB; A0A0R1U9F6; -.
DR   STRING; 1423763.FC46_GL000455; -.
DR   PATRIC; fig|1423763.3.peg.459; -.
DR   OrthoDB; 250531at2; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000051036; Unassembled WGS sequence.
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; GHMP kinase, C-terminal domain; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00131; gal_kin; 1.
DR   PANTHER; PTHR10457:SF35; GALACTOKINASE; 1.
DR   PANTHER; PTHR10457; MEVALONATE KINASE/GALACTOKINASE; 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   PRINTS; PR00959; MEVGALKINASE.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00106; GALACTOKINASE; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00246};
KW   Galactose metabolism {ECO:0000256|ARBA:ARBA00023144, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00246};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00246};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00246}.
FT   DOMAIN          8..57
FT                   /note="Galactokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10509"
FT   DOMAIN          115..182
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          286..366
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         33..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   SITE            27
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
SQ   SEQUENCE   387 AA;  43421 MW;  C3C7D670DFD538CE CRC64;
     MNKDELLKEY VETFGEKGQD VFFSPGRINV IGEHTDYNGG HVFPAAISLG VYGVYGPRDD
     KKVRLFSGNV NGNIVEFDID DTTVEKGERF WANYFKGMIT YLREKYDNID HGFNLYIKAN
     LPSGSGLSSS AAIEMLMGII LKDEFKLDVD RVNLAKMGQR TENEFVGLNS GIMDQFACIM
     GKKDSAIFLD CNTLEYEYLP LELGNYEIII MATNKPHTLA DSAYNDRVRE CHDALTKLQE
     KLDIKALGEL DNDTFDEYSY LINDKTELKR ARHAVSENQR AIRATKAMKD GDLEKIGRLI
     NASHISLHYD YEVTGKELDT LAEASWKQDG VLGARMIGGG FGGSAIAIVK KDKAEEFKKN
     VGKTYRDKIG YDASFYDAEI VDGSKMI
//
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