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Database: UniProt
Entry: B2G9P6
LinkDB: B2G9P6
Original site: B2G9P6 
ID   GAL1_LACRJ              Reviewed;         392 AA.
AC   B2G9P6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   29-OCT-2014, entry version 46.
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=LAR_1662;
OS   Lactobacillus reuteri (strain JCM 1112).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H.,
RA   Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H.,
RA   Kikuchi J., Masaoka T., Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and
RT   Lactobacillus fermentum reveal a genomic island for reuterin and
RT   cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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: ATP + alpha-D-galactose = ADP + alpha-D-
CC       galactose 1-phosphate. {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; AP007281; BAG26178.1; -; Genomic_DNA.
DR   RefSeq; YP_001842658.1; NC_010609.1.
DR   ProteinModelPortal; B2G9P6; -.
DR   SMR; B2G9P6; 5-392.
DR   STRING; 557433.LAR_1662; -.
DR   EnsemblBacteria; BAG26178; BAG26178; LAR_1662.
DR   GeneID; 6230905; -.
DR   KEGG; lrf:LAR_1662; -.
DR   PATRIC; 22260999; VBILacReu111271_1833.
DR   eggNOG; COG0153; -.
DR   HOGENOM; HOG000241101; -.
DR   KO; K00849; -.
DR   OMA; HAILLMC; -.
DR   OrthoDB; EOG6DG2SH; -.
DR   BioCyc; LREU557433:GHNR-1743-MONOMER; -.
DR   UniPathway; UPA00214; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004335; F:galactokinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-HAMAP.
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; 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   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   PRINTS; PR00959; MEVGALKINASE.
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; Complete proteome; Cytoplasm;
KW   Galactose metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    392       Galactokinase.
FT                                /FTId=PRO_1000100833.
FT   NP_BIND     129    135       ATP. {ECO:0000255|HAMAP-Rule:MF_00246}.
FT   REGION       33     36       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   ACT_SITE    179    179       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   METAL       135    135       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   METAL       167    167       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   BINDING      67     67       ATP. {ECO:0000255|HAMAP-Rule:MF_00246}.
FT   BINDING     229    229       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00246}.
FT   SITE         27     27       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00246}.
SQ   SEQUENCE   392 AA;  44056 MW;  2877C04471F8200A CRC64;
     MDKQQFLAEY QDVFKEPGKD VFFSPGRINV IGEHTDYNGG HVFPCAISIG TYGVYGPRED
     TTVAIYSANS AKEEDSKIIT FDINDTEPQN AKDEKWVNYF KGMLVYLKQR GFKIDHGFNL
     YIHGFLPYGS GLSSSASIEM LMGNILKDEF NLDIDEIELV KLGQKTENDF VGLNSGIMDQ
     FAVGMGKENN AIYLDCNTLE YKYLPLELGD YEIIIMSTNK NHSLAGSKYN ERVQECEEAV
     KRLNKKLDIN KLGELDSDTF DQYTYLIDDD TLIRRARHAV SENERTKKAI DAMEKGDLEE
     LGRLINASHV SLKYDYEVTG KELDTLAENA WNQPGCLGAR MVGGGFAGSA IAIVKKSEAE
     NFKKNVGKIY RDKIGYDASF YDAEVVDGPH KL
//
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