ID A0A0S7XN49_9BACT Unreviewed; 389 AA.
AC A0A0S7XN49;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Galactokinase {ECO:0000256|HAMAP-Rule:MF_00246};
DE EC=2.7.1.6 {ECO:0000256|HAMAP-Rule:MF_00246};
DE AltName: Full=Galactose kinase {ECO:0000256|HAMAP-Rule:MF_00246};
GN Name=galK {ECO:0000256|HAMAP-Rule:MF_00246};
GN ORFNames=AMK68_03565 {ECO:0000313|EMBL:KPJ63603.1};
OS candidate division KD3-62 bacterium DG_56.
OC Bacteria; candidate division KD3-62.
OX NCBI_TaxID=1704032 {ECO:0000313|EMBL:KPJ63603.1, ECO:0000313|Proteomes:UP000052020};
RN [1] {ECO:0000313|EMBL:KPJ63603.1, ECO:0000313|Proteomes:UP000052020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_56 {ECO:0000313|EMBL:KPJ63603.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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|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:KPJ63603.1}.
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; LIZY01000075; KPJ63603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XN49; -.
DR PATRIC; fig|1704032.3.peg.541; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000052020; 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:SF7; GALACTOKINASE-RELATED; 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 7..55
FT /note="Galactokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10509"
FT DOMAIN 112..176
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 280..360
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 31..34
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 119..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT SITE 25
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
SQ SEQUENCE 389 AA; 42169 MW; 57BAC6BC8F01E099 CRC64;
MEAIGDQFAE TFGHREYRLF RAPGRVNLIG EHTDYNDGFV LPVAIDHDIL VAASPRSDRT
ICAYSTNFDC HITFSLDHIE SDADHPWSNY LRGVAFFLEE AGLRPGGFDA VYEGNVPIGA
GLSSSAALEV VTAFALQGLF GFEMGPEEMA LLCQRAENDF VGMHCGIMDQ FVSRLGQAGH
ALFLDCRSLA HKAVPLAAGD PCIVICDTGV KRELAGSEYN VRREQCEAGV ALLQERLPEV
RALRDVTVEQ LRAHADSLPS PIRERCAHVV EENDRVMRSL ACLRAGDLSG FGRLMNDSHV
SLRDQYQVSS PELDTLVDTA LAVPGTLGSR MTGAGFGGCT VSLVVADALD EFKQRVVAAY
RERFGRDPDI YLTSAVDGAG ELLVPASAS
//