GAL1_PYRFU
ID GAL1_PYRFU Reviewed; 352 AA.
AC Q9HHB6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=PF0445;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RA Verhees C.H.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11978175; DOI=10.1042/bj20011597;
RA Verhees C.H., Koot D.G., Ettema T.J., Dijkema C., de Vos W.M.,
RA van der Oost J.;
RT "Biochemical adaptations of two sugar kinases from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL Biochem. J. 366:121-127(2002).
RN [4]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=14501125; DOI=10.1107/s090744490301607x;
RA de Geus D., Hartley A.P., Sedelnikova S.E., Glynn S.E., Baker P.J.,
RA Verhees C.H., van der Oost J., Rice D.W.;
RT "Cloning, purification, crystallization and preliminary crystallographic
RT analysis of galactokinase from Pyrococcus furiosus.";
RL Acta Crystallogr. D 59:1819-1821(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH MG-ADP AND SUBSTRATE,
RP ACTIVE SITE, REACTION MECHANISM, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=15003454; DOI=10.1016/j.jmb.2004.01.043;
RA Hartley A., Glynn S.E., Barynin V., Baker P.J., Sedelnikova S.E.,
RA Verhees C.H., de Geus D., van der Oost J., Timson D.J., Reece R.J.,
RA Rice D.W.;
RT "Substrate specificity and mechanism from the structure of Pyrococcus
RT furiosus galactokinase.";
RL J. Mol. Biol. 337:387-398(2004).
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). Is very
CC specific for its substrate, since it is not able to use D-glucose, D-
CC fructose, D-mannose, 2-deoxy-D-glucose, and D-glucosamine as
CC substrates. {ECO:0000255|HAMAP-Rule:MF_00246,
CC ECO:0000269|PubMed:11978175}.
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 ECO:0000269|PubMed:11978175};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 mM for D-galactose (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11978175};
CC KM=0.006 mM for ATP (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11978175};
CC KM=0.27 mM for D-galactose (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:11978175};
CC KM=0.008 mM for ATP (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:11978175};
CC Vmax=3.66 umol/min/mg enzyme (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11978175};
CC Vmax=43.2 umol/min/mg enzyme (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:11978175};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:11978175};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:11978175};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00246}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11978175,
CC ECO:0000269|PubMed:14501125, ECO:0000269|PubMed:15003454}.
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; AF195244; AAG28454.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80569.1; -; Genomic_DNA.
DR RefSeq; WP_011011563.1; NC_018092.1.
DR PDB; 1S4E; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I=1-352.
DR PDBsum; 1S4E; -.
DR AlphaFoldDB; Q9HHB6; -.
DR SMR; Q9HHB6; -.
DR STRING; 186497.PF0445; -.
DR EnsemblBacteria; AAL80569; AAL80569; PF0445.
DR GeneID; 41712245; -.
DR KEGG; pfu:PF0445; -.
DR PATRIC; fig|186497.12.peg.469; -.
DR eggNOG; arCOG01029; Archaea.
DR HOGENOM; CLU_017814_2_1_2; -.
DR OMA; NTHQDYK; -.
DR OrthoDB; 65810at2157; -.
DR PhylomeDB; Q9HHB6; -.
DR UniPathway; UPA00214; -.
DR EvolutionaryTrace; Q9HHB6; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004335; F:galactokinase activity; IDA:UniProtKB.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006012; P:galactose metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Cytoplasm;
KW Galactose metabolism; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..352
FT /note="Galactokinase"
FT /id="PRO_0000184641"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15003454"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15003454"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15003454"
FT BINDING 101..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:15003454"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15003454"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15003454"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246,
FT ECO:0000269|PubMed:15003454"
FT SITE 11
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:15003454"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:1S4E"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1S4E"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 196..214
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 232..256
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 307..316
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:1S4E"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:1S4E"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1S4E"
SQ SEQUENCE 352 AA; 39375 MW; 44413EAEDEE518B7 CRC64;
MSKITVKSPG RVNLIGEHTD YTYGYVMPMA IDLYTIITAE KYDKVQLYSE HFNEEKTFTL
DNLTKEGSWI DYVKGVLWVL IQEGYKIGGL KGKITGDLPL GAGLSSSASF EVGILEVLNQ
LYNLNIDPLK KALLAKKAEN EFVGVPCGIL DQFAVVFGKK DNVIFLDTQT LQYEYIPFPK
DVSVLVFYTG VKRELASSEY AERKRIAEES LRILGKESSK EVTEKDLGKL PPLHRKFFSY
IVRENARVLE VRDALKEGDI EKVGKILTTA HWDLAENYRV SCEELDFFVK KAMELGAYGA
RLTGAGFGGS AIALVDKDKA KTIGDAILRE YLAKFSWKAK YFVVKPSDGV GV
