ID A0A1M6BNX4_9CLOT Unreviewed; 387 AA.
AC A0A1M6BNX4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN02745163_00409 {ECO:0000313|EMBL:SHI50366.1};
OS Clostridium cavendishii DSM 21758.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHI50366.1, ECO:0000313|Proteomes:UP000184310};
RN [1] {ECO:0000313|EMBL:SHI50366.1, ECO:0000313|Proteomes:UP000184310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21758 {ECO:0000313|EMBL:SHI50366.1,
RC ECO:0000313|Proteomes:UP000184310};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZB01000003; SHI50366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6BNX4; -.
DR STRING; 1121302.SAMN02745163_00409; -.
DR OrthoDB; 250531at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000184310; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184310};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00246}.
FT DOMAIN 8..55
FT /note="Galactokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10509"
FT DOMAIN 113..180
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 284..358
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 32..35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 123..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT SITE 26
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
SQ SEQUENCE 387 AA; 43358 MW; F78CE64C19AA42EF CRC64;
MLDVLKSDFK EIFKVNAENI FFAPGRVNLI GEHTDYNGGH VFPCALSFGT YAVSRKREDG
LVRMYSLNFE DLGIIEFSIN DLQNIKQDDW ANYPKGVIWA FKEKGYSINH GMDVLVYGNI
PNGAGLSSSA SIELVTSVML KDYFDLDLDM IEMVKLSQMA ENKFIGVNCG IMDQFAIGMG
KENHAILLDT NNLKYEYVPV SLDGASIVIA NTNKRRGLAD SKYNERRSEC EEALSDIKEH
KDINSLGDLT EEEFINLKQY IKRDVCRDRA EHAVLENIRT KKAVEVLKQG KISEFGELMK
SSHYSLKDKY EVTGIELDTL VELALEERGV IGSRMTGAGF GGCTISLVKN ENIEDFVKNV
GKGYKEKIGY EASFYVASVG DGARKLF
//
