GAL1_THEMA
ID GAL1_THEMA Reviewed; 350 AA.
AC P56838; O33837;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=TM_1190;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9741105; DOI=10.1016/s0723-2020(98)80002-7;
RA Liebl W., Wagner B., Schellhase J.;
RT "Properties of an alpha-galactosidase, and structure of its gene galA,
RT within an alpha- and beta-galactoside utilization gene cluster of the
RT hyperthermophilic bacterium Thermotoga maritima.";
RL Syst. Appl. Microbiol. 21:1-11(1998).
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; AE000512; AAD36265.1; -; Genomic_DNA.
DR EMBL; AJ001072; CAA04516.1; -; Genomic_DNA.
DR PIR; C72283; C72283.
DR RefSeq; NP_228995.1; NC_000853.1.
DR RefSeq; WP_004080140.1; NZ_CP011107.1.
DR AlphaFoldDB; P56838; -.
DR SMR; P56838; -.
DR STRING; 243274.THEMA_08380; -.
DR EnsemblBacteria; AAD36265; AAD36265; TM_1190.
DR KEGG; tma:TM1190; -.
DR eggNOG; COG0153; Bacteria.
DR InParanoid; P56838; -.
DR OMA; PVCYNLR; -.
DR OrthoDB; 1388391at2; -.
DR BioCyc; MetaCyc:MON-505; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004335; F:galactokinase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006012; P:galactose metabolic process; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..350
FT /note="Galactokinase"
FT /id="PRO_0000184631"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 14..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 96..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT SITE 8
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
SQ SEQUENCE 350 AA; 39589 MW; 4ADA4705151B7695 CRC64;
MKVKAPGRIN IIGEHTDYND GYVLPFAVNR YVFLSIEGSE RFIFHSENVN ETVEMEKIEK
LNKWTDYISG VIASFEKRGY RVSPVKISVS SNLPIGAGLS SSAALEVATA YAISEYFGFN
VPKLELVKIA REAEVEFVGV RCGIMDQFTA VFGKKDHAIF LDTMTLEYEY VPLKLEGYEI
NLVDSNVKHE LSSSEYNRRR QECEEVLKTL EKKSFREVTK EDLERLSGTL RKRAQHVLEE
NERVLKSVQA LKEGDFETLG KLLFSSHESL RDLYEVSCEE TDFIVDYLRG KEGILGARMV
GGGFGGGVIV LSKKGAFGKI KEELVESYRK RFGIDLIFHE IESSDGVQKI
