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Entry: A0A1G9WTQ7_9BACT
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Original site: A0A1G9WTQ7_9BACT 
ID   A0A1G9WTQ7_9BACT        Unreviewed;       386 AA.
AC   A0A1G9WTQ7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Galactokinase {ECO:0000256|HAMAP-Rule:MF_00246};
DE            EC=2.7.1.6 {ECO:0000256|HAMAP-Rule:MF_00246};
DE   AltName: Full=Galactose kinase {ECO:0000256|HAMAP-Rule:MF_00246};
GN   Name=galK {ECO:0000256|HAMAP-Rule:MF_00246};
GN   ORFNames=SAMN04488090_4437 {ECO:0000313|EMBL:SDM87974.1};
OS   Siphonobacter aquaeclarae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=563176 {ECO:0000313|EMBL:SDM87974.1, ECO:0000313|Proteomes:UP000198901};
RN   [1] {ECO:0000313|EMBL:SDM87974.1, ECO:0000313|Proteomes:UP000198901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21668 {ECO:0000313|EMBL:SDM87974.1,
RC   ECO:0000313|Proteomes:UP000198901};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_00246};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00246}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00246}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000256|ARBA:ARBA00006566, ECO:0000256|HAMAP-Rule:MF_00246}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00246}.
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DR   EMBL; FNGS01000010; SDM87974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9WTQ7; -.
DR   STRING; 563176.SAMN04488090_4437; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000198901; Unassembled WGS sequence.
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: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; GHMP kinase, C-terminal domain; 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; IPR006206; Mevalonate/galactokinase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00131; gal_kin; 1.
DR   PANTHER; PTHR10457:SF7; GALACTOKINASE-RELATED; 1.
DR   PANTHER; PTHR10457; MEVALONATE KINASE/GALACTOKINASE; 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   PRINTS; PR00959; MEVGALKINASE.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00106; GALACTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00246};
KW   Galactose metabolism {ECO:0000256|ARBA:ARBA00023144, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00246};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00246};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00246};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00246}; Reference proteome {ECO:0000313|Proteomes:UP000198901};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00246}.
FT   DOMAIN          11..59
FT                   /note="Galactokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10509"
FT   DOMAIN          113..179
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          284..363
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         35..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         122..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT   SITE            29
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
SQ   SEQUENCE   386 AA;  43429 MW;  28F9FE2BBD7F9099 CRC64;
     MEPLTQSIVD RYRTLFGADP SLIVRSPGRI NLIGEHTDYN MGFVLPAAID REMVFAISPR
     TDRLCRAYAF NLEREETFSL DNLTRSEERW TYYLKGVIDQ ILQLGYDLKG CDVVFGGNIP
     LGAGISSSAA LEAGFSFALN EIFQLGIDRM TLVRLCQRAE NQFVGVNCGI MDMFASLMGA
     EDAVIRLDCR SLDYEYFPFR QEEHILILCD TGVKHSLGNS EYNTRRAECE RGVALLQAYD
     ASVNSLRDVS PELLRAHRDE FDEVTYRRCE YMVEEIARVV AACEDLKRDD LVSFGKHMYA
     THYGLQHKYE VSCPELDFLV DQTRNQPAVL GARMMGGGFG GCTINLVEKT AADAFLETMK
     TAYQAAFGIE LVCHKVVIRQ GTSVVR
//
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