GAL1_LACLA
ID GAL1_LACLA Reviewed; 399 AA.
AC Q9R7D7; O87521;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=LL1983;
GN ORFNames=L0028;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7962;
RA Lee J.M., Chung D.K., Park J.H., Lee W.K., Chang H.C., Kim J.H., Lee H.J.;
RT "The organization of genes involved in metabolism of gal/lac of Lactococcus
RT lactis.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-399.
RC STRAIN=NCDO 2054;
RX PubMed=9733693; DOI=10.1128/jb.180.18.4893-4902.1998;
RA Vaughan E.E., Pridmore R.D., Mollet B.;
RT "Transcriptional regulation and evolution of lactose genes in the
RT galactose-lactose operon of Lactococcus lactis NCDO2054.";
RL J. Bacteriol. 180:4893-4902(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP PHOSPHATE, FUNCTION, ACTIVE SITE, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=12796487; DOI=10.1074/jbc.m304789200;
RA Thoden J.B., Holden H.M.;
RT "Molecular structure of galactokinase.";
RL J. Biol. Chem. 278:33305-33311(2003).
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:0000305|PubMed:12796487}.
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 -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:12796487}.
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; U60828; AAD11510.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK06081.1; -; Genomic_DNA.
DR EMBL; AF082008; AAC63017.1; -; Genomic_DNA.
DR PIR; G86872; G86872.
DR RefSeq; NP_268140.1; NC_002662.1.
DR RefSeq; WP_010906249.1; NC_002662.1.
DR PDB; 1PIE; X-ray; 2.10 A; A=1-399.
DR PDBsum; 1PIE; -.
DR AlphaFoldDB; Q9R7D7; -.
DR SMR; Q9R7D7; -.
DR STRING; 272623.L0028; -.
DR PaxDb; Q9R7D7; -.
DR EnsemblBacteria; AAK06081; AAK06081; L0028.
DR GeneID; 60355907; -.
DR KEGG; lla:L0028; -.
DR PATRIC; fig|272623.7.peg.2136; -.
DR eggNOG; COG0153; Bacteria.
DR HOGENOM; CLU_017814_2_1_9; -.
DR OMA; PVCYNLR; -.
DR UniPathway; UPA00214; -.
DR EvolutionaryTrace; Q9R7D7; -.
DR Proteomes; UP000002196; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Cytoplasm;
KW Galactose metabolism; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..399
FT /note="Galactokinase"
FT /id="PRO_0000184615"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:12796487"
FT BINDING 42..45
FT /ligand="substrate"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 133..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246,
FT ECO:0000269|PubMed:12796487"
FT SITE 36
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="T -> A (in Ref. 3; AAC63017)"
FT /evidence="ECO:0000305"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:1PIE"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 50..66
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1PIE"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 231..250
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 274..299
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 302..318
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1PIE"
FT HELIX 363..378
FT /evidence="ECO:0007829|PDB:1PIE"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:1PIE"
SQ SEQUENCE 399 AA; 43825 MW; D013EA01C4CE2EA8 CRC64;
MSIVVENSTV LSALTEKFAE VFGDTKEVEY FFSPGRINLI GEHTDYNGGY VFPASITIGT
TGLARLREDK KVKLYSENFP KLGVIEFDLD EVEKKDGELW SNYVKGMIVM LKGAGYEIDK
GFELLIKGEI PTASGLSSSA SLELLVGVVL DDLFNLNVPR LELVQLGQKT ENDYIGVNSG
ILDQFAIGFG EVKKAILLDC NTLKYEMVPV ELRDYDIVIM NTNKPRALTE SKYNERFAET
REALKRMQTR LDIQSLGELS NEEFDANTDL IGDETLIKRA RHAVYENNRT KIAQKAFVAG
NLTKFGELLN ASHASLKDDY EVTGLELDTL AETAQKQAGV LGARMTGAGF GGCAIALVAH
DNVSAFEKAV GQVYEEVVGY PASFYVAQIG SGSTKLDVE
