GALK1_MOUSE
ID GALK1_MOUSE Reviewed; 392 AA.
AC Q9R0N0; Q9JIA6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Galactokinase;
DE EC=2.7.1.6 {ECO:0000269|PubMed:10915771};
DE AltName: Full=Galactose kinase;
GN Name=Galk1; Synonyms=Galk, Glk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10915771; DOI=10.1093/hmg/9.12.1821;
RA Ai Y., Zheng Z., O'Brien-Jenkins A., Bernard D.J., Wynshaw-Boris T.,
RA Ning C., Reynolds R., Segal S., Huang K., Stambolian D.;
RT "A mouse model of galactose-induced cataracts.";
RL Hum. Mol. Genet. 9:1821-1827(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse galactokinase (galK).";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:10915771}.
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:10915771};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13554;
CC Evidence={ECO:0000305|PubMed:10915771};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000305|PubMed:10915771}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51570}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC {ECO:0000305}.
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DR EMBL; AF246459; AAF78226.1; -; Genomic_DNA.
DR EMBL; AB027012; BAA84705.1; -; mRNA.
DR EMBL; AK045694; BAC32460.1; -; mRNA.
DR EMBL; AK168716; BAE40558.1; -; mRNA.
DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34544.1; -; Genomic_DNA.
DR EMBL; BC016602; AAH16602.1; -; mRNA.
DR CCDS; CCDS25654.1; -.
DR RefSeq; NP_058601.2; NM_016905.2.
DR AlphaFoldDB; Q9R0N0; -.
DR SMR; Q9R0N0; -.
DR BioGRID; 199945; 3.
DR IntAct; Q9R0N0; 4.
DR MINT; Q9R0N0; -.
DR STRING; 10090.ENSMUSP00000021114; -.
DR iPTMnet; Q9R0N0; -.
DR PhosphoSitePlus; Q9R0N0; -.
DR SwissPalm; Q9R0N0; -.
DR EPD; Q9R0N0; -.
DR jPOST; Q9R0N0; -.
DR MaxQB; Q9R0N0; -.
DR PaxDb; Q9R0N0; -.
DR PRIDE; Q9R0N0; -.
DR ProteomicsDB; 273413; -.
DR Antibodypedia; 2046; 292 antibodies from 32 providers.
DR DNASU; 14635; -.
DR Ensembl; ENSMUST00000021114; ENSMUSP00000021114; ENSMUSG00000020766.
DR GeneID; 14635; -.
DR KEGG; mmu:14635; -.
DR UCSC; uc007mjn.1; mouse.
DR CTD; 2584; -.
DR MGI; MGI:95730; Galk1.
DR VEuPathDB; HostDB:ENSMUSG00000020766; -.
DR eggNOG; KOG0631; Eukaryota.
DR GeneTree; ENSGT00950000183187; -.
DR HOGENOM; CLU_017814_2_0_1; -.
DR InParanoid; Q9R0N0; -.
DR OMA; NTHQDYK; -.
DR OrthoDB; 860024at2759; -.
DR PhylomeDB; Q9R0N0; -.
DR TreeFam; TF354326; -.
DR Reactome; R-MMU-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR BioGRID-ORCS; 14635; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Galk1; mouse.
DR PRO; PR:Q9R0N0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9R0N0; protein.
DR Bgee; ENSMUSG00000020766; Expressed in yolk sac and 234 other tissues.
DR Genevisible; Q9R0N0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004335; F:galactokinase activity; IDA:MGI.
DR GO; GO:0005534; F:galactose binding; ISO:MGI.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISO:MGI.
DR GO; GO:0019402; P:galactitol metabolic process; IMP:MGI.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:MGI.
DR GO; GO:0006012; P:galactose metabolic process; IDA:MGI.
DR GO; GO:0061623; P:glycolytic process from galactose; IMP:MGI.
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 1: Evidence at protein 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_0000184646"
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"
FT CONFLICT 19..20
FT /note="AF -> V (in Ref. 1; BAA84705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42295 MW; 068432AD97CDDDFE CRC64;
MAAWRPPRVE ELLAEARRAF MEEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELV
TVMVGSPRTD GLVSLLTTSK DADEPQRLQF PLPSAQWSLE PGIPQWANYV KGVIQHYPAS
PLVGFSAVVV SSVPLGGGLS SSASLEVATY TFIQQLCPDS GAIAARAQVC QRAEHSFAGV
PCGIMDQLIA LLGQKGYALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LGSSEYPVRR
RQCEEVAQAL GKESLREVRM EELEAGRELM SKEGFRRARH VVSEIRRTAQ AAAAMSRGDY
KAFGRLMVES HYSLRDDYEV SCPELDQLVE AALSVPGVYG SRMTGGGFGG CTVTLLEASV
APLVIDHIQE QYSGTATFYL SQAADGAQVL SL
