ID GALK1_HUMAN Reviewed; 392 AA. AC P51570; B2RC07; B4E1G6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 221. DE RecName: Full=Galactokinase {ECO:0000305}; DE EC=2.7.1.6 {ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:7542884}; DE AltName: Full=Galactose kinase; GN Name=GALK1 {ECO:0000312|HGNC:HGNC:4118}; Synonyms=GALK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GALAC2 MET-32. RX PubMed=7670469; DOI=10.1038/ng0795-307; RA Stambolian D., Ai Y., Sidjanin D., Nesburn K., Sathe G., Rosenberg M., RA Bergsma D.J.; RT "Cloning of the galactokinase cDNA and identification of mutations in two RT families with cataracts."; RL Nat. Genet. 10:307-312(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8908517; DOI=10.1101/gr.6.10.980; RA Bergsma D.J., Ai Y., Skach W.R., Nesburn K., Anoia E., van Horn S., RA Stambolian D.; RT "Fine structure of the human galactokinase GALK1 gene."; RL Genome Res. 6:980-985(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 6-17; 22-37; 70-97; 205-239; 257-267; 288-296 AND RP 343-388, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7542884; DOI=10.1006/bbrc.1995.2023; RA Ai Y., Basu M., Bergsma D.J., Stambolian D.; RT "Comparison of the enzymatic activities of human galactokinase GALK1 and a RT related human galactokinase protein GK2."; RL Biochem. Biophys. Res. Commun. 212:687-691(1995). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-392 IN COMPLEX WITH D-GALACTOSE RP AND ATP ANALOG, SUBUNIT, AND SUBSTRATE-BINDING SITES. RX PubMed=15590630; DOI=10.1074/jbc.m412916200; RA Thoden J.B., Timson D.J., Reece R.J., Holden H.M.; RT "Molecular structure of human galactokinase: implications for type II RT galactosemia."; RL J. Biol. Chem. 280:9662-9670(2005). RN [14] RP VARIANT GALAC2 THR-28. RX PubMed=10521295; DOI=10.1086/302611; RA Kalaydjieva L., Perez-Lezaun A., Angelicheva D., Onengut S., Dye D., RA Bosshard N.U., Jordanova A., Savov A., Yanakiev P., Kremensky I., RA Radeva B., Hallmayer J., Markov A., Nedkova V., Tournev I., Aneva L., RA Gitzelmann R.; RT "A founder mutation in the GK1 gene is responsible for galactokinase RT deficiency in Roma (Gypsies)."; RL Am. J. Hum. Genet. 65:1299-1307(1999). RN [15] RP VARIANTS GALAC2 THR-28; ARG-36; TYR-44; SER-346 AND SER-349. RX PubMed=10790206; RX DOI=10.1002/(sici)1098-1004(200005)15:5<447::aid-humu6>3.0.co;2-m; RA Kolosha V., Anoia E., de Cespedes C., Gitzelmann R., Shih L., Casco T., RA Saborio M., Trejos R., Buist N., Tedesco T., Skach W., Mitelmann O., RA Ledee D., Huang K., Stambolian D.; RT "Novel mutations in 13 probands with galactokinase deficiency."; RL Hum. Mutat. 15:447-453(2000). RN [16] RP VARIANT GALAC2 VAL-198. RX PubMed=11231902; DOI=10.1086/319512; RA Okano Y., Asada M., Fujimoto A., Ohtake A., Murayama K., Hsiao K.-J., RA Choeh K., Yang Y., Cao Q., Reichardt J.K.V., Niihira S., Imamura T., RA Yamano T.; RT "A genetic factor for age-related cataract: identification and RT characterization of a novel galactokinase variant, 'Osaka,' in Asians."; RL Am. J. Hum. Genet. 68:1036-1042(2001). RN [17] RP VARIANTS GALAC2 CYS-68; MET-288 AND PRO-384. RX PubMed=11139256; DOI=10.1002/1098-1004(2001)17:1<77::aid-humu20>3.0.co;2-h; RA Hunter M., Angelicheva D., Levy H.L., Pueschel S.M., Kalaydjieva L.; RT "Novel mutations in the GALK1 gene in patients with galactokinase RT deficiency."; RL Hum. Mutat. 17:77-78(2001). RN [18] RP CHARACTERIZATION OF VARIANTS GALAC2 THR-28; MET-32; ARG-36; TYR-44; CYS-68; RP VAL-198; MET-288; SER-346; SER-349 AND PRO-384, CATALYTIC ACTIVITY, RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12694189; DOI=10.1046/j.1432-1033.2003.03538.x; RA Timson D.J., Reece R.J.; RT "Functional analysis of disease-causing mutations in human galactokinase."; RL Eur. J. Biochem. 270:1767-1774(2003). RN [19] RP VARIANTS MET-184; ASP-274 AND ALA-338. RX PubMed=12942049; RA Maraini G., Hejtmancik J.F., Shiels A., Mackay D.S., Aldigeri R., RA Jiao X.D., Williams S.L., Sperduto R.D., Reed G.; RT "Galactokinase gene mutations and age-related cataract. Lack of association RT in an Italian population."; RL Mol. Vis. 9:397-400(2003). RN [20] RP VARIANTS GALAC2 MET-32 AND GLN-239. RX PubMed=15024738; DOI=10.1002/humu.9223; RA Sangiuolo F., Magnani M., Stambolian D., Novelli G.; RT "Biochemical characterization of two GALK1 mutations in patients with RT galactokinase deficiency."; RL Hum. Mutat. 23:396-396(2004). 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:0000269|PubMed:12694189, CC ECO:0000269|PubMed:7542884}. 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:0000269|PubMed:12694189, ECO:0000269|PubMed:7542884}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13554; CC Evidence={ECO:0000305|PubMed:7542884}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=970 uM for alpha-D-galactose {ECO:0000269|PubMed:12694189}; CC KM=34 uM for ATP {ECO:0000269|PubMed:12694189}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC {ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:7542884}. CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15590630}. CC -!- INTERACTION: CC P51570; Q9NPJ4: PNRC2; NbExp=3; IntAct=EBI-2269932, EBI-726549; CC -!- DISEASE: Galactosemia 2 (GALAC2) [MIM:230200]: A form of galactosemia, CC an inborn error of galactose metabolism typically manifesting in the CC neonatal period, after ingestion of galactose, with jaundice, CC hepatosplenomegaly, hepatocellular insufficiency, food intolerance, CC hypoglycemia, renal tubular dysfunction, muscle hypotonia, sepsis and CC cataract. GALAC2 inheritance is autosomal recessive. CC {ECO:0000269|PubMed:10521295, ECO:0000269|PubMed:10790206, CC ECO:0000269|PubMed:11139256, ECO:0000269|PubMed:11231902, CC ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:15024738, CC ECO:0000269|PubMed:7670469}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG64778.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW89316.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Galactosemia Proteins Database; CC URL="http://www.protein-variants.eu/galactosemia/"; 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; U26401; AAA96147.1; -; mRNA. DR EMBL; L76927; AAB51607.1; -; Genomic_DNA. DR EMBL; AK303832; BAG64778.1; ALT_INIT; mRNA. DR EMBL; AK314890; BAG37404.1; -; mRNA. DR EMBL; BT007005; AAP35651.1; -; mRNA. DR EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471099; EAW89316.1; ALT_INIT; Genomic_DNA. DR EMBL; BC001166; AAH01166.1; -; mRNA. DR CCDS; CCDS11728.1; -. DR RefSeq; NP_000145.1; NM_000154.1. DR PDB; 1WUU; X-ray; 2.50 A; A/B/C/D=2-392. DR PDB; 6GR2; X-ray; 2.49 A; A/B/C/D/E/F/G/H=2-392. DR PDB; 6Q3W; X-ray; 1.96 A; A/B/C/D=2-392. DR PDB; 6Q3X; X-ray; 2.10 A; A/B=2-392. DR PDB; 6Q8Z; X-ray; 2.40 A; A/B/C/D=2-392. DR PDB; 6Q90; X-ray; 2.40 A; A/B/C/D=2-392. DR PDB; 6Q91; X-ray; 2.40 A; A/B/C/D=2-392. DR PDB; 6QJE; X-ray; 2.40 A; A/B/C/D=2-392. DR PDB; 6ZFH; X-ray; 2.44 A; A/B/C/D/E/F/G/H=2-392. DR PDB; 6ZGV; X-ray; 2.30 A; A/B/D/E=2-392. DR PDB; 6ZGW; X-ray; 2.30 A; A/B/D/E=2-392. DR PDB; 6ZGX; X-ray; 1.86 A; A/B/D/E=2-392. DR PDB; 6ZGY; X-ray; 2.30 A; A/B/D/E=2-392. DR PDB; 6ZGZ; X-ray; 2.30 A; A/B/D/E=2-392. DR PDB; 6ZH0; X-ray; 2.50 A; A/B/D/E=2-392. DR PDB; 7OZX; X-ray; 2.30 A; A/B/C/D=2-392. DR PDB; 7RCL; X-ray; 2.40 A; A/B/C/D=1-392. DR PDB; 7RCM; X-ray; 2.10 A; A/B=1-392. DR PDB; 7S49; X-ray; 2.20 A; A/B=1-392. DR PDB; 7S4C; X-ray; 2.20 A; A/B=1-392. DR PDBsum; 1WUU; -. DR PDBsum; 6GR2; -. DR PDBsum; 6Q3W; -. DR PDBsum; 6Q3X; -. DR PDBsum; 6Q8Z; -. DR PDBsum; 6Q90; -. DR PDBsum; 6Q91; -. DR PDBsum; 6QJE; -. DR PDBsum; 6ZFH; -. DR PDBsum; 6ZGV; -. DR PDBsum; 6ZGW; -. DR PDBsum; 6ZGX; -. DR PDBsum; 6ZGY; -. DR PDBsum; 6ZGZ; -. DR PDBsum; 6ZH0; -. DR PDBsum; 7OZX; -. DR PDBsum; 7RCL; -. DR PDBsum; 7RCM; -. DR PDBsum; 7S49; -. DR PDBsum; 7S4C; -. DR AlphaFoldDB; P51570; -. DR SMR; P51570; -. DR BioGRID; 108857; 74. DR IntAct; P51570; 37. DR MINT; P51570; -. DR STRING; 9606.ENSP00000225614; -. DR BindingDB; P51570; -. DR ChEMBL; CHEMBL1293257; -. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR GlyGen; P51570; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P51570; -. DR PhosphoSitePlus; P51570; -. DR BioMuta; GALK1; -. DR DMDM; 1730187; -. DR OGP; P51570; -. DR REPRODUCTION-2DPAGE; IPI00019383; -. DR CPTAC; CPTAC-375; -. DR CPTAC; CPTAC-376; -. DR EPD; P51570; -. DR jPOST; P51570; -. DR MassIVE; P51570; -. DR MaxQB; P51570; -. DR PaxDb; 9606-ENSP00000465930; -. DR PeptideAtlas; P51570; -. DR Pumba; P51570; -. DR Antibodypedia; 2046; 313 antibodies from 32 providers. DR DNASU; 2584; -. DR Ensembl; ENST00000225614.6; ENSP00000225614.1; ENSG00000108479.13. DR Ensembl; ENST00000588479.6; ENSP00000465930.1; ENSG00000108479.13. DR GeneID; 2584; -. DR KEGG; hsa:2584; -. DR MANE-Select; ENST00000588479.6; ENSP00000465930.1; NM_000154.2; NP_000145.1. DR AGR; HGNC:4118; -. DR CTD; 2584; -. DR DisGeNET; 2584; -. DR GeneCards; GALK1; -. DR HGNC; HGNC:4118; GALK1. DR HPA; ENSG00000108479; Tissue enhanced (liver). DR MalaCards; GALK1; -. DR MIM; 230200; phenotype. DR MIM; 604313; gene. DR neXtProt; NX_P51570; -. DR OpenTargets; ENSG00000108479; -. DR Orphanet; 79237; Galactokinase deficiency. DR PharmGKB; PA28533; -. DR VEuPathDB; HostDB:ENSG00000108479; -. DR eggNOG; KOG0631; Eukaryota. DR GeneTree; ENSGT00950000183187; -. DR HOGENOM; CLU_017814_2_0_1; -. DR InParanoid; P51570; -. DR OMA; VMPCAIN; -. DR OrthoDB; 177392at2759; -. DR PhylomeDB; P51570; -. DR TreeFam; TF354326; -. DR BioCyc; MetaCyc:HS03112-MONOMER; -. DR BRENDA; 2.7.1.6; 2681. DR PathwayCommons; P51570; -. DR Reactome; R-HSA-5609976; Defective GALK1 causes GALCT2. DR Reactome; R-HSA-70370; Galactose catabolism. DR SABIO-RK; P51570; -. DR SignaLink; P51570; -. DR UniPathway; UPA00214; -. DR BioGRID-ORCS; 2584; 35 hits in 1156 CRISPR screens. DR EvolutionaryTrace; P51570; -. DR GenomeRNAi; 2584; -. DR Pharos; P51570; Tbio. DR PRO; PR:P51570; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P51570; Protein. DR Bgee; ENSG00000108479; Expressed in right lobe of liver and 97 other cell types or tissues. DR ExpressionAtlas; P51570; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. 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:0019402; P:galactitol metabolic process; IEA:Ensembl. DR GO; GO:0019388; P:galactose catabolic process; TAS:Reactome. DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:Ensembl. DR GO; GO:0006012; P:galactose metabolic process; IMP: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; GHMP kinase, C-terminal domain; 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_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. DR Genevisible; P51570; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Carbohydrate metabolism; Cataract; KW Direct protein sequencing; Disease variant; Galactose metabolism; Kinase; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..392 FT /note="Galactokinase" FT /id="PRO_0000184645" FT ACT_SITE 186 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9HHB6" FT BINDING 37 FT /ligand="alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:28061" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 43 FT /ligand="alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:28061" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 44 FT /ligand="alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:28061" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 46 FT /ligand="alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:28061" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 138 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 140 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 141 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 186 FT /ligand="alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:28061" FT /evidence="ECO:0000250|UniProtKB:P04385" FT BINDING 236 FT /ligand="alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:28061" FT /evidence="ECO:0000250|UniProtKB:P04385" FT SITE 37 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:Q9HHB6" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 28 FT /note="P -> T (in GALAC2; founder Romani mutation; FT dbSNP:rs104894572)" FT /evidence="ECO:0000269|PubMed:10521295, FT ECO:0000269|PubMed:10790206, ECO:0000269|PubMed:12694189" FT /id="VAR_008514" FT VARIANT 32 FT /note="V -> M (in GALAC2; dbSNP:rs104894576)" FT /evidence="ECO:0000269|PubMed:12694189, FT ECO:0000269|PubMed:15024738, ECO:0000269|PubMed:7670469" FT /id="VAR_002547" FT VARIANT 36 FT /note="G -> R (in GALAC2)" FT /evidence="ECO:0000269|PubMed:10790206, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023486" FT VARIANT 44 FT /note="H -> Y (in GALAC2; dbSNP:rs1555748926)" FT /evidence="ECO:0000269|PubMed:10790206, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023487" FT VARIANT 68 FT /note="R -> C (in GALAC2; dbSNP:rs1365349586)" FT /evidence="ECO:0000269|PubMed:11139256, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023488" FT VARIANT 184 FT /note="I -> M (in dbSNP:rs773416476)" FT /evidence="ECO:0000269|PubMed:12942049" FT /id="VAR_023489" FT VARIANT 198 FT /note="A -> V (in GALAC2; mild deficiency; Osaka; FT dbSNP:rs80084721)" FT /evidence="ECO:0000269|PubMed:11231902, FT ECO:0000269|PubMed:12694189" FT /id="VAR_015746" FT VARIANT 239 FT /note="R -> Q (in GALAC2; dbSNP:rs575139300)" FT /evidence="ECO:0000269|PubMed:15024738" FT /id="VAR_023490" FT VARIANT 274 FT /note="G -> D (in dbSNP:rs959842362)" FT /evidence="ECO:0000269|PubMed:12942049" FT /id="VAR_023491" FT VARIANT 288 FT /note="T -> M (in GALAC2; dbSNP:rs759284637)" FT /evidence="ECO:0000269|PubMed:11139256, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023492" FT VARIANT 338 FT /note="V -> A" FT /evidence="ECO:0000269|PubMed:12942049" FT /id="VAR_023493" FT VARIANT 346 FT /note="G -> S (in GALAC2; dbSNP:rs375690568)" FT /evidence="ECO:0000269|PubMed:10790206, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023494" FT VARIANT 349 FT /note="G -> S (in GALAC2; dbSNP:rs754967473)" FT /evidence="ECO:0000269|PubMed:10790206, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023495" FT VARIANT 384 FT /note="A -> P (in GALAC2; dbSNP:rs1184406839)" FT /evidence="ECO:0000269|PubMed:11139256, FT ECO:0000269|PubMed:12694189" FT /id="VAR_023496" FT HELIX 9..24 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 29..39 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 54..67 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 69..77 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:1WUU" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:6Q3X" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:6ZH0" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1WUU" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 141..156 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 163..178 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 185..192 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:6ZGX" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 218..228 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 231..249 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 260..265 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 272..296 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 300..316 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 323..333 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 338..343 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 348..357 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:6ZGX" FT HELIX 361..371 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:6ZGY" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:6ZGX" FT STRAND 387..391 FT /evidence="ECO:0007829|PDB:6ZGX" SQ SEQUENCE 392 AA; 42272 MW; 8D7CFF8FDB0E4718 CRC64; MAALRQPQVA ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELM TVLVGSPRKD GLVSLLTTSE GADEPQRLQF PLPTAQRSLE PGTPRWANYV KGVIQYYPAA PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GTIAARAQVC QQAEHSFAGM PCGIMDQFIS LMGQKGHALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LASSEYPVRR RQCEEVARAL GKESLREVQL EELEAARDLV SKEGFRRARH VVGEIRRTAQ AAAALRRGDY RAFGRLMVES HRSLRDDYEV SCPELDQLVE AALAVPGVYG SRMTGGGFGG CTVTLLEASA APHAMRHIQE HYGGTATFYL SQAADGAKVL CL //