GAL1_PASMU
ID GAL1_PASMU Reviewed; 385 AA.
AC P57899;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=PM1035;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03119.1; -; Genomic_DNA.
DR RefSeq; WP_010906982.1; NC_002663.1.
DR AlphaFoldDB; P57899; -.
DR SMR; P57899; -.
DR STRING; 747.DR93_934; -.
DR EnsemblBacteria; AAK03119; AAK03119; PM1035.
DR KEGG; pmu:PM1035; -.
DR PATRIC; fig|272843.6.peg.1048; -.
DR HOGENOM; CLU_017814_2_1_6; -.
DR OMA; PVCYNLR; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000809; Chromosome.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..385
FT /note="Galactokinase"
FT /id="PRO_0000184620"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 34..37
FT /ligand="substrate"
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 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT SITE 28
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
SQ SEQUENCE 385 AA; 41923 MW; 9297DD8EFE42F0DF CRC64;
MTPQQSAQRL FQEKFNCTPT LNVYAPGRVN IIGEHTDYND GFVMPCAINY GTAISGRKRD
DSRFKVYAGD LQQWDEFDLA QEITPDSSKK WTGYVRGVVK FVQTHCPDFK CGADLVISGN
VPLSAGLSSS ASLEVAVGKF CQQLGNLPLT NTEIALIGQK AENQFVGCQC GNMDQLISAL
GQKDHLLMID CRSLETIPTP IPANVAVMIV NSHVKHDLVA GEYNTRRQQC EVAAKFFGVK
ALRDVSLAQF KQREAELTAL DPEVAKRARH VVTENQRVLD AVKALQSGNL ALLGELMAQS
HESMRDDFEI TVPQIDYLVE LAQIAIGKTG GARMTGGGFG GCIVAVAPVE KVEAVRQIIA
DNYAQQTGLK EDFYVCTASQ GVSVC
