(data stored in SCRATCH zone)

SWISSPROT: D6XXA1_BACIE

ID   D6XXA1_BACIE            Unreviewed;       388 AA.
AC   D6XXA1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Galactokinase {ECO:0000256|HAMAP-Rule:MF_00246, ECO:0000256|SAAS:SAAS00080100};
DE            EC=2.7.1.6 {ECO:0000256|HAMAP-Rule:MF_00246, ECO:0000256|SAAS:SAAS00015833};
DE   AltName: Full=Galactose kinase {ECO:0000256|HAMAP-Rule:MF_00246};
GN   Name=galK {ECO:0000256|HAMAP-Rule:MF_00246};
GN   OrderedLocusNames=Bsel_0419 {ECO:0000313|EMBL:ADH97958.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97958.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97958.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00246, ECO:0000256|SAAS:SAAS00541114}.
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:0000256|HAMAP-
CC         Rule:MF_00246, ECO:0000256|SAAS:SAAS01118323};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00246, ECO:0000256|SAAS:SAAS00015843}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00246,
CC       ECO:0000256|SAAS:SAAS00345504}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00246, ECO:0000256|SAAS:SAAS00544826}.
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DR   EMBL; CP001791; ADH97958.1; -; Genomic_DNA.
DR   RefSeq; WP_013171387.1; NC_014219.1.
DR   STRING; 439292.Bsel_0419; -.
DR   EnsemblBacteria; ADH97958; ADH97958; Bsel_0419.
DR   KEGG; bse:Bsel_0419; -.
DR   eggNOG; ENOG4105CRD; Bacteria.
DR   eggNOG; COG0153; LUCA.
DR   HOGENOM; HOG000241101; -.
DR   KO; K00849; -.
DR   OMA; YECSHPD; -.
DR   OrthoDB; 1388391at2; -.
DR   BioCyc; BSEL439292:G1GLR-449-MONOMER; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000000271; 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; D6XXA1.
DR   SWISS-2DPAGE; D6XXA1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00456406};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00132170}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00423689};
KW   Galactose metabolism {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00132176};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00456396, ECO:0000313|EMBL:ADH97958.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00423699};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00423702};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00456300};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00246,
KW   ECO:0000256|SAAS:SAAS00456450, ECO:0000313|EMBL:ADH97958.1}.
FT   DOMAIN        7     57       GalKase_gal_bdg. {ECO:0000259|Pfam:
FT                                PF10509}.
FT   DOMAIN      114    181       GHMP_kinases_N. {ECO:0000259|Pfam:
FT                                PF00288}.
FT   DOMAIN      285    365       GHMP_kinases_C. {ECO:0000259|Pfam:
FT                                PF08544}.
FT   NP_BIND     124    130       ATP. {ECO:0000256|HAMAP-Rule:MF_00246}.
FT   REGION       33     36       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00246}.
FT   COILED      221    241       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    174    174       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00246}.
FT   METAL       130    130       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00246}.
FT   METAL       162    162       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00246}.
FT   BINDING      67     67       ATP. {ECO:0000256|HAMAP-Rule:MF_00246}.
FT   BINDING     224    224       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00246}.
FT   SITE         27     27       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00246}.
SQ   SEQUENCE   388 AA;  43563 MW;  A4CB06A801A6D899 CRC64;
     MIDHLKQEFD KIFHESGELR YFFAPGRVNL IGEHIDYNGG YVFPTALDVG TYLAVRKRSD
     RKLRFYSENF PQMGIVEGDL DDLAYSQADD WVSYAKGVLY MFMEEGMTGD KGFDVYVFGN
     IPNGAGLSSS ASIELAFAVM WDAVNGFSMD RVTMVKLCQR AENEYIGVNC GIMDQFAIGF
     GKKEHAVLLD CDTLDYEYAR LKLDGYKILI ANTNKRRGLA DSKYNERRQE CETALSELQE
     KEVVSHLCEL DEAAFNEASH LIKGADRLKR ARHAVTENER TKKAFRALED GDLPAFGQLM
     NDSHVSLRDD YEVTGKELDA MVEAAWQEET VIGARMTGAG FGGCTVNIVK EDGLDETVKR
     ISQRYTDQTG IEPKFYVVTT GDGAKELT
//

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