ID A0A1C5J4D8_9ACTN Unreviewed; 385 AA.
AC A0A1C5J4D8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Galactokinase {ECO:0000256|ARBA:ARBA00012315, ECO:0000256|HAMAP-Rule:MF_00246};
DE EC=2.7.1.6 {ECO:0000256|ARBA:ARBA00012315, ECO:0000256|HAMAP-Rule:MF_00246};
DE AltName: Full=Galactose kinase {ECO:0000256|ARBA:ARBA00029590, ECO:0000256|HAMAP-Rule:MF_00246};
GN Name=galK {ECO:0000256|HAMAP-Rule:MF_00246};
GN ORFNames=GA0070614_3956 {ECO:0000313|EMBL:SCG65442.1};
OS Micromonospora coxensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG65442.1, ECO:0000313|Proteomes:UP000198215};
RN [1] {ECO:0000313|EMBL:SCG65442.1, ECO:0000313|Proteomes:UP000198215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG65442.1,
RC ECO:0000313|Proteomes:UP000198215};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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|ARBA:ARBA00004947, 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}.
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DR EMBL; LT607753; SCG65442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5J4D8; -.
DR OrthoDB; 250531at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000198215; Chromosome i.
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; IPR006203; GHMP_knse_ATP-bd_CS.
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:SF35; GALACTOKINASE; 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.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00246}.
FT DOMAIN 11..59
FT /note="Galactokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10509"
FT DOMAIN 115..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 174
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 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 124..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 226
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 385 AA; 40185 MW; E491F3C70D53FF3C CRC64;
MTDVAARATA GFRSAYGQQP AGRWAAPGRA NLIGEHTDYN DGFVLPFALS LRTVVAASPQ
PGERWTAFSE TTDQPVEFGA AEADEPGRVT GWGAYVAGVV WALREAGYAV PGARLAIASD
VPLGSGLSSS AALEAAVLAA LVDLGGLDLP AERRPRLAQR AENAYVGAPT GIMDQSAVIR
CREGHALFLD CRTEAVEHIP FDLDAAGLAM LVVDSRAPHR HADGEYASRR KSCEAAASAL
GVPALRDVAV ADLDAALGRL PDDETRRRVR HVVTEDQRVL DTVALLRAGR VREIGPLLTA
SHASMRDDFE ITVPEIDTAV EAALAAGALG ARMTGGGFGG CVLALVEAAS ATTVADAVTR
AYAERGFTTP RHVTVLPAPG ATRLP
//
