GALK1_CANLF
ID GALK1_CANLF Reviewed; 392 AA.
AC Q9GKK4;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Galactokinase;
DE EC=2.7.1.6 {ECO:0000250|UniProtKB:P51570};
DE AltName: Full=Galactose kinase;
GN Name=GALK1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sidjanin D.J.;
RT "Identification and analysis of canine galactokinase (GALK1) cDNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12620391; DOI=10.1016/s0888-7543(02)00028-9;
RA Sidjanin D.J., Miller B., Kijas J., McElwee J., Pillardy J., Malek J.,
RA Pai G., Feldblyum T., Fraser C., Acland G., Aguirre G.;
RT "Radiation hybrid map, physical map, and low-pass genomic sequence of the
RT canine prcd region on CFA9 and comparative mapping with the syntenic region
RT on human chromosome 17.";
RL Genomics 81:138-148(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Graves K.T., Ennis R.B.;
RT "Exon scan of the canine galactokinase (GALK1) gene in dog breeds affected
RT with juvenile cataract.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a phosphate from ATP to alpha-D-
CC galactose and participates in the first committed step in the
CC catabolism of galactose. {ECO:0000250|UniProtKB:P51570}.
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:0000250|UniProtKB:P51570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13554;
CC Evidence={ECO:0000250|UniProtKB:P51570};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000250|UniProtKB:P51570}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51570}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF213513; AAG43832.1; -; mRNA.
DR EMBL; AF454963; AAO15527.1; -; Genomic_DNA.
DR EMBL; AY267338; AAP31026.1; -; Genomic_DNA.
DR RefSeq; NP_001003104.1; NM_001003104.2.
DR AlphaFoldDB; Q9GKK4; -.
DR SMR; Q9GKK4; -.
DR STRING; 9612.ENSCAFP00000007327; -.
DR PaxDb; Q9GKK4; -.
DR PRIDE; Q9GKK4; -.
DR Ensembl; ENSCAFT00030008166; ENSCAFP00030007172; ENSCAFG00030004437.
DR GeneID; 403694; -.
DR KEGG; cfa:403694; -.
DR CTD; 2584; -.
DR eggNOG; KOG0631; Eukaryota.
DR HOGENOM; CLU_017814_2_0_1; -.
DR InParanoid; Q9GKK4; -.
DR OMA; NTHQDYK; -.
DR OrthoDB; 860024at2759; -.
DR TreeFam; TF354326; -.
DR BRENDA; 2.7.1.6; 1153.
DR Reactome; R-CFA-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000004914; Expressed in granulocyte and 46 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004335; F:galactokinase activity; ISS:UniProtKB.
DR GO; GO:0005534; F:galactose binding; ISS:UniProtKB.
DR GO; GO:0019402; P:galactitol metabolic process; IEA:Ensembl.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:Ensembl.
DR GO; GO:0006012; P:galactose metabolic process; ISS:UniProtKB.
DR GO; GO:0061623; P:glycolytic process from galactose; IEA:Ensembl.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR000705; Galactokinase.
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 2: Evidence at transcript level;
KW ATP-binding; Carbohydrate metabolism; Galactose metabolism; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..392
FT /note="Galactokinase"
FT /id="PRO_0000184644"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 43..46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 183..186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51570"
SQ SEQUENCE 392 AA; 42121 MW; 8FD5ECF3AB4386BF CRC64;
MAASSPPRAG ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELV
TVLVGSPRAD GLVSLLTTSE DADEPRRLQF PLPTAQRSLE PGTPRWANYV KGVIQHYPAA
PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GSVAARAQVC QQAEHSFAGV
PCGIMDQLIA LLGQEGHALL IDCRSLETSL VPLSEPKLAV LITNSNVRHS LGSSEYPLRR
RQCEEVARAL GKESLREVQL EELEAGRELV SKEGFRRARH VVGEIRRTAQ AAAALCRGDY
RAFGRLMVES HHSLRDDYEV SCPELDQLVE AALSAPGVYG SRMTGGGFGG CTVTLLEASF
TSQVMQHIQE QYSGTATFYL SQAADGAKVL HW
