(data stored in ACNUC7421 zone)

SWISSPROT: GAL1_EXIS2

ID   GAL1_EXIS2              Reviewed;         390 AA.
AC   B1YIH8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 77.
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=Exig_0377;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001022; ACB59861.1; -; Genomic_DNA.
DR   RefSeq; WP_012369285.1; NC_010556.1.
DR   SMR; B1YIH8; -.
DR   STRING; 262543.Exig_0377; -.
DR   EnsemblBacteria; ACB59861; ACB59861; Exig_0377.
DR   KEGG; esi:Exig_0377; -.
DR   eggNOG; ENOG4105CRD; Bacteria.
DR   eggNOG; COG0153; LUCA.
DR   HOGENOM; HOG000241101; -.
DR   KO; K00849; -.
DR   OMA; YECSHPD; -.
DR   OrthoDB; 1388391at2; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000001681; 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; B1YIH8.
DR   SWISS-2DPAGE; B1YIH8.
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..390
FT                   /note="Galactokinase"
FT                   /id="PRO_1000100830"
FT   NP_BIND         124..130
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   REGION          33..36
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   METAL           130
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   METAL           162
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         67
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         224
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   SITE            27
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
SQ   SEQUENCE   390 AA;  43211 MW;  90453F43F59B0C9E CRC64;
     MTDQTLEQIF EQQFGQSSTH RFFAPGRINL IGEHTDYNGG HVFPCALTLG THAVARKRDD
     VVFRFYSLNF EDDGIIEVAG DDLTPQSAHG WANYAKGMIH VLREAGYRID TGCDILIKGD
     IPNGAGLSSS ASLELVIGVL LDKLYNLDID RIDLVKYGQQ VENQYIGVNS GIMDQFAIGM
     GKAGSGLLLD CETLDYTYAP LDLSGYTIII MNTNKRRELA DSKYNERRSE CEAALAYLQQ
     YRPYASLGQW SMNEFETVSF EDERLERRAR HAISENERTL QALDALKEDR LEAFGQLMNA
     SHRSLRVDYE VTGKELDTLV EAAWAQPGVL GARMTGAGFG GCAIAIVEDD TVETFMTAVG
     HAYETEIGYP ASFYTATVGD GAREVEQEVI
//

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