GAL1_PYRHO
ID GAL1_PYRHO Reviewed; 350 AA.
AC O58107;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
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=PH0369;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND CRYSTALLIZATION.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16511293; DOI=10.1107/s1744309106001813;
RA Inagaki E., Sakamoto K., Obayashi N., Terada T., Shirouzu M., Bessho Y.,
RA Kuroishi C., Kuramitsu S., Shinkai A., Yokoyama S.;
RT "Expression, purification, crystallization and preliminary X-ray
RT diffraction analysis of galactokinase from Pyrococcus horikoshii.";
RL Acta Crystallogr. F 62:169-171(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP SUBSTRATE AND AN ATP ANALOG.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of galactokinase from Pyrococcus horikoshii.";
RL Submitted (JUL-2011) to the PDB data bank.
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, ECO:0000269|PubMed:16511293}.
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:16511293};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=403 uM for D-galactose {ECO:0000269|PubMed:16511293};
CC KM=132 uM for ATP {ECO:0000269|PubMed:16511293};
CC Note=kcat is 0.91 sec(-1).;
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; BA000001; BAA29443.1; -; Genomic_DNA.
DR PIR; F71144; F71144.
DR RefSeq; WP_010884456.1; NC_000961.1.
DR PDB; 2CZ9; X-ray; 1.50 A; A=1-350.
DR PDB; 2DEI; X-ray; 1.70 A; A=1-350.
DR PDB; 2DEJ; X-ray; 1.50 A; A=1-350.
DR PDBsum; 2CZ9; -.
DR PDBsum; 2DEI; -.
DR PDBsum; 2DEJ; -.
DR AlphaFoldDB; O58107; -.
DR SMR; O58107; -.
DR STRING; 70601.3256760; -.
DR PRIDE; O58107; -.
DR EnsemblBacteria; BAA29443; BAA29443; BAA29443.
DR GeneID; 1444243; -.
DR KEGG; pho:PH0369; -.
DR eggNOG; arCOG01029; Archaea.
DR OMA; NTHQDYK; -.
DR OrthoDB; 65810at2157; -.
DR UniPathway; UPA00214; -.
DR EvolutionaryTrace; O58107; -.
DR Proteomes; UP000000752; Chromosome.
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; -; 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 Transferase.
FT CHAIN 1..350
FT /note="Galactokinase"
FT /id="PRO_0000184642"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 15..18
FT /ligand="substrate"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 99..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT BINDING 198
FT /ligand="substrate"
FT SITE 9
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 23..47
FT /evidence="ECO:0007829|PDB:2CZ9"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2CZ9"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2DEI"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 230..254
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2CZ9"
FT HELIX 318..332
FT /evidence="ECO:0007829|PDB:2CZ9"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2CZ9"
SQ SEQUENCE 350 AA; 39342 MW; E2B165005F1CB7D7 CRC64;
MIKVKSPGRV NLIGEHTDYT YGYVMPMAIN LYTKIEAEKH GEVILYSEHF GEERKFSLND
LRKENSWIDY VKGIFWVLKE SDYEVGGIKG RVSGNLPLGA GLSSSASFEV GILETLDKLY
NLKLDSLSKV LLAKKAENEF VGVPCGILDQ FAVVFGREGN VIFLDTHTLD YEYIPFPKDV
SILVFYTGVR RELASSEYAE RKHIAEESLK ILGKGSSKEV REGELSKLPP LHRKFFGYIV
RENARVLEVR DALKEGNVEE VGKILTTAHW DLAKNYEVSC KELDFFVERA LKLGAYGARL
TGAGFGGSAI ALVDKEDAET IGEEILREYL KRFPWKARHF IVEPSDGVGI
