GAL1_FUSNN
ID GAL1_FUSNN Reviewed; 389 AA.
AC Q8RHD0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=FN2107;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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}.
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DR EMBL; AE009951; AAL94191.1; -; Genomic_DNA.
DR RefSeq; NP_602892.1; NC_003454.1.
DR AlphaFoldDB; Q8RHD0; -.
DR SMR; Q8RHD0; -.
DR STRING; 190304.FN2107; -.
DR PRIDE; Q8RHD0; -.
DR EnsemblBacteria; AAL94191; AAL94191; FN2107.
DR KEGG; fnu:FN2107; -.
DR PATRIC; fig|190304.8.peg.569; -.
DR eggNOG; COG0153; Bacteria.
DR HOGENOM; CLU_017814_2_1_0; -.
DR InParanoid; Q8RHD0; -.
DR OMA; PVCYNLR; -.
DR BioCyc; FNUC190304:G1FZS-592-MON; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004335; F:galactokinase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006012; P:galactose metabolic process; IBA:GO_Central.
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_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_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;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..389
FT /note="Galactokinase"
FT /id="PRO_0000184611"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 33..36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 124..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 224
FT /ligand="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 389 AA; 43753 MW; 784257843B31D98E CRC64;
MLENLIKDFK EIFKYSGEVE RFFSPGRVNL IGEHTDYNGG FVFPCALDFG TYAVVKKRED
KTFKMYSKNF ENLGIIEFNL DNLIYDKKDD WANYPKGVIK TFLDRNYKID SGFDVLFFGN
IPNGAGLSSS ASIEVLTAVI LKDLFKLDVD IIEMVKMCQV AENKFIGVNS GIMDQFAVGM
GKKDNAILLD CNTLKYEYVP VKLVNMSIVI ANTNKKRGLA DSKYNERRTS CEEAVKVLNN
NEVNIKYLGE LTVTEFEKVK HYITDEEQLK RATHAVTENE RAKIAVEFLK KDDIAEFGKL
MNKSHTSLRD DYEVTGLELD SLVEAAWEEK GTVGSRMTGA GFGGCTVSIV ENDYVDSFIK
NVGKKYKEKT GLEASFYIAN IGDGAGKVK
