(data stored in ACNUC7421 zone)

SWISSPROT: GAL1_ECO27

ID   GAL1_ECO27              Reviewed;         382 AA.
AC   B7ULN0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
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};
GN   OrderedLocusNames=E2348C_0634;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to
CC       D-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-
CC         phosphate + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28061, ChEBI:CHEBI:30616, ChEBI:CHEBI:58336,
CC         ChEBI:CHEBI:456216; EC=2.7.1.6; Evidence={ECO:0000255|HAMAP-
CC         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}.
DR   EMBL; FM180568; CAS08182.1; -; Genomic_DNA.
DR   RefSeq; WP_000053454.1; NC_011601.1.
DR   SMR; B7ULN0; -.
DR   PRIDE; B7ULN0; -.
DR   EnsemblBacteria; CAS08182; CAS08182; E2348C_0634.
DR   KEGG; ecg:E2348C_0634; -.
DR   KO; K00849; -.
DR   OMA; YECSHPD; -.
DR   BioCyc; ECOL574521:E2348C_RS03405-MONOMER; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000008205; 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:0005534; F:galactose binding; IEA:InterPro.
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_gal-bd.
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;
DR   PRODOM; B7ULN0.
DR   SWISS-2DPAGE; B7ULN0.
KW   ATP-binding; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW   Galactose metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    382       Galactokinase.
FT                                /FTId=PRO_1000125377.
FT   NP_BIND     124    130       ATP. {ECO:0000255|HAMAP-Rule:MF_00246}.
FT   REGION       34     37       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   ACT_SITE    174    174       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   METAL       130    130       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   METAL       162    162       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   SITE         28     28       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00246}.
SQ   SEQUENCE   382 AA;  41461 MW;  0721C08EDCCDD958 CRC64;
     MSLKEKTQSL FANAFGYPAT RTIQAPGRVN 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
//

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