ID A0A1A7P2M7_9PAST Unreviewed; 384 AA.
AC A0A1A7P2M7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=QS62_03670 {ECO:0000313|EMBL:OBW95479.1}, QV08_07595
GN {ECO:0000313|EMBL:OBX07294.1};
OS Gallibacterium salpingitidis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=505341 {ECO:0000313|EMBL:OBW95479.1, ECO:0000313|Proteomes:UP000092649};
RN [1] {ECO:0000313|Proteomes:UP000092603, ECO:0000313|Proteomes:UP000092649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19987/2 Salp {ECO:0000313|EMBL:OBX07294.1,
RC ECO:0000313|Proteomes:UP000092603}, and F150
RC {ECO:0000313|EMBL:OBW95479.1, ECO:0000313|Proteomes:UP000092649};
RA Kudirkiene E., Bojesen A.M.;
RT "Pan-genome of Gallibacterium spp.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00246}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBW95479.1}.
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DR EMBL; JTJL01000012; OBW95479.1; -; Genomic_DNA.
DR EMBL; JTJT01000036; OBX07294.1; -; Genomic_DNA.
DR RefSeq; WP_066106069.1; NZ_JTJT01000036.1.
DR AlphaFoldDB; A0A1A7P2M7; -.
DR STRING; 505341.QV08_07595; -.
DR PATRIC; fig|505341.3.peg.742; -.
DR OrthoDB; 250531at2; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000092603; Unassembled WGS sequence.
DR Proteomes; UP000092649; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000092649};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00246}.
FT DOMAIN 10..55
FT /note="Galactokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10509"
FT DOMAIN 114..180
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 280..363
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 123..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
FT BINDING 161
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 28
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00246"
SQ SEQUENCE 384 AA; 42208 MW; B1F1BBF3F817E70B CRC64;
MNPIQQSKQV FIERFAVQPT LQVYAPGRVN LIGEHTDYND GFVMPCAINY GTAICGNLRD
DHQFYVFAAD LNETDQFSLI EEIKPVDRKW CNYIRGVVHF IQQACPEFKQ GANLVISGNV
PLSSGLSSSA ALEVATGKFC QQLGNLALTN TELALIGQKS ENIFVGCQCG NMDQLISALG
QEHHALMIDC RSLDTVPTPI PDNLAVMIVN SHVKHDLVDG EYNTRRQQCE QAAAFFGVKA
LRDVTVEQFN AKGDELAAAN PLAYKRAKHV VTENQRVLEA VEALKHNDIT RLGELMAQSH
DSMRDDFEIT VPEIDYLVEL AQLVIGKTGG ARMTGGGFGG CIVAIAPHNK VEAVRKIIAD
NYHKQTGLKE DFYVCTASQG VHLC
//
