GAL1_ECOLI
ID GAL1_ECOLI Reviewed; 382 AA.
AC P0A6T3; P06976;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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}; Synonyms=galA;
GN OrderedLocusNames=b0757, JW0740;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3158881; DOI=10.1093/nar/13.6.1841;
RA Debouck C., Riccio A., Schumperli D., McKenney K., Jeffers J., Hughes C.,
RA Rosenberg M., Heusterspreute M., Brunel F., Davison J.;
RT "Structure of the galactokinase gene of Escherichia coli, the last (?) gene
RT of the gal operon.";
RL Nucleic Acids Res. 13:1841-1853(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=SA1310;
RX PubMed=200486; DOI=10.1016/0014-5793(77)80638-8;
RA Schlesinger D.H., Schell M.A., Wilson D.B.;
RT "The NH2-terminal sequences of galactokinase from Escherichia coli and
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 83:45-47(1977).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-382.
RX PubMed=7966338; DOI=10.1006/jmbi.1994.1728;
RA Bouffard G.G., Rudd K.E., Adhya S.L.;
RT "Dependence of lactose metabolism upon mutarotase encoded in the gal operon
RT in Escherichia coli.";
RL J. Mol. Biol. 244:269-278(1994).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP PARAMETERS.
RC STRAIN=K12;
RX PubMed=12816414; DOI=10.1021/ol034642d;
RA Yang J., Fu X., Jia Q., Shen J., Biggins J.B., Jiang J., Zhao J.,
RA Schmidt J.J., Wang P.G., Thorson J.S.;
RT "Studies on the substrate specificity of Escherichia coli galactokinase.";
RL Org. Lett. 5:2223-2226(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND MUTAGENESIS OF TYR-371.
RC STRAIN=K12;
RX PubMed=14612558; DOI=10.1073/pnas.100.23.13184;
RA Hoffmeister D., Yang J., Liu L., Thorson J.S.;
RT "Creation of the first anomeric D/L-sugar kinase by means of directed
RT evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13184-13189(2003).
RN [9]
RP 3D-STRUCTURE MODELING.
RX PubMed=21423888; DOI=10.6026/97320630005422;
RA Sharma A., Malakar P.;
RT "Comparative modeling and genomics for galactokinase (Gal1p) enzyme.";
RL Bioinformation 5:422-429(2011).
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). To a lesser
CC extent, is also able to phosphorylate 2-deoxy-D-galactose and D-
CC galactosamine. Is not able to use D-galacturonic acid, D-talose, L-
CC altrose, and L-glucose as substrates. {ECO:0000255|HAMAP-Rule:MF_00246,
CC ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558,
CC ECO:0000269|PubMed:200486}.
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 ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558,
CC ECO:0000269|PubMed:200486};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 mM for D-galactose {ECO:0000269|PubMed:12816414,
CC ECO:0000269|PubMed:14612558};
CC KM=3.6 mM for 2-deoxy-D-galactose {ECO:0000269|PubMed:12816414,
CC ECO:0000269|PubMed:14612558};
CC KM=2.9 mM for D-galactosamine {ECO:0000269|PubMed:12816414,
CC ECO:0000269|PubMed:14612558};
CC KM=2.5 mM for ATP {ECO:0000269|PubMed:12816414,
CC ECO:0000269|PubMed:14612558};
CC Vmax=1.65 umol/min/mg enzyme with D-galactose as substrate
CC {ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558};
CC Note=kcat is 108 min(-1), 30 min(-1) and 11.7 min(-1) with D-
CC galactose, 2-deoxy-D-galactose, and D-galactosamine as substrate,
CC respectively.;
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}.
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; X02306; CAA26172.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73844.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35419.1; -; Genomic_DNA.
DR EMBL; U13636; AAB17019.1; -; Genomic_DNA.
DR PIR; B23044; KIECGG.
DR RefSeq; NP_415278.1; NC_000913.3.
DR RefSeq; WP_000053415.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P0A6T3; -.
DR SMR; P0A6T3; -.
DR BioGRID; 4261711; 225.
DR BioGRID; 849734; 4.
DR IntAct; P0A6T3; 4.
DR STRING; 511145.b0757; -.
DR jPOST; P0A6T3; -.
DR PaxDb; P0A6T3; -.
DR PRIDE; P0A6T3; -.
DR EnsemblBacteria; AAC73844; AAC73844; b0757.
DR EnsemblBacteria; BAA35419; BAA35419; BAA35419.
DR GeneID; 66670972; -.
DR GeneID; 945358; -.
DR KEGG; ecj:JW0740; -.
DR KEGG; eco:b0757; -.
DR PATRIC; fig|1411691.4.peg.1521; -.
DR EchoBASE; EB0358; -.
DR eggNOG; COG0153; Bacteria.
DR HOGENOM; CLU_017814_2_1_6; -.
DR InParanoid; P0A6T3; -.
DR OMA; PVCYNLR; -.
DR PhylomeDB; P0A6T3; -.
DR BioCyc; EcoCyc:GALACTOKIN-MON; -.
DR BioCyc; MetaCyc:GALACTOKIN-MON; -.
DR SABIO-RK; P0A6T3; -.
DR UniPathway; UPA00214; -.
DR PHI-base; PHI:6269; -.
DR PRO; PR:P0A6T3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004335; F:galactokinase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Galactose metabolism; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:200486"
FT CHAIN 2..382
FT /note="Galactokinase"
FT /id="PRO_0000184607"
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"
FT MUTAGEN 371
FT /note="Y->H: Displays relaxed substrate specificity since
FT it gains kinase activity toward sugars as diverse as D-
FT galacturonic acid, D-talose, L-altrose, and L-glucose. Also
FT shows enhanced turnover of the small pool of sugars
FT converted by the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:14612558"
SQ SEQUENCE 382 AA; 41442 MW; 7D886CE6FC48F0A1 CRC64;
MSLKEKTQSL FANAFGYPAT HTIQAPGRVN LIGEHTDYND GFVLPCAIDY QTVISCAPRD
DRKVRVMAAD YENQLDEFSL DAPIVAHENY QWANYVRGVV KHLQLRNNSF GGVDMVISGN
VPQGAGLSSS ASLEVAVGTV LQQLYHLPLD GAQIALNGQE AENQFVGCNC GIMDQLISAL
GKKDHALLID CRSLGTKAVS MPKGVAVVII NSNFKRTLVG SEYNTRREQC ETGARFFQQP
ALRDVTIEEF NAVAHELDPI VAKRVRHILT ENARTVEAAS ALEQGDLKRM GELMAESHAS
MRDDFEITVP QIDTLVEIVK AVIGDKGGVR MTGGGFGGCI VALIPEELVP AVQQAVAEQY
EAKTGIKETF YVCKPSQGAG QC
