GALM_MOUSE
ID GALM_MOUSE Reviewed; 342 AA.
AC Q8K157;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Galactose mutarotase;
DE EC=5.1.3.3 {ECO:0000250|UniProtKB:Q96C23};
DE AltName: Full=Aldose 1-epimerase;
GN Name=Galm {ECO:0000312|MGI:MGI:2442420};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: Mutarotase that catalyzes the interconversion of beta-D-
CC galactose and alpha-D-galactose during galactose metabolism. Beta-D-
CC galactose is metabolized in the liver into glucose 1-phosphate, the
CC primary metabolic fuel, by the action of four enzymes that constitute
CC the Leloir pathway: GALM, GALK1 (galactokinase), GALT (galactose-1-
CC phosphate uridylyltransferase) and GALE (UDP-galactose-4'-epimerase).
CC Involved in the maintenance of the equilibrium between the beta- and
CC alpha-anomers of galactose, therefore ensuring a sufficient supply of
CC the alpha-anomer for GALK1. Also active on D-glucose although shows a
CC preference for galactose over glucose. {ECO:0000250|UniProtKB:Q96C23}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose = beta-D-galactose; Xref=Rhea:RHEA:28675,
CC ChEBI:CHEBI:27667, ChEBI:CHEBI:28061; EC=5.1.3.3;
CC Evidence={ECO:0000250|UniProtKB:Q96C23};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28677;
CC Evidence={ECO:0000250|UniProtKB:Q96C23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC Evidence={ECO:0000250|UniProtKB:Q96C23};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:Q96C23}.
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000250|UniProtKB:Q96C23}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96C23}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR EMBL; AK040998; BAC30776.1; -; mRNA.
DR EMBL; BC028818; AAH28818.1; -; mRNA.
DR CCDS; CCDS28987.1; -.
DR RefSeq; NP_795937.1; NM_176963.4.
DR AlphaFoldDB; Q8K157; -.
DR SMR; Q8K157; -.
DR STRING; 10090.ENSMUSP00000040580; -.
DR iPTMnet; Q8K157; -.
DR PhosphoSitePlus; Q8K157; -.
DR REPRODUCTION-2DPAGE; Q8K157; -.
DR EPD; Q8K157; -.
DR jPOST; Q8K157; -.
DR MaxQB; Q8K157; -.
DR PaxDb; Q8K157; -.
DR PeptideAtlas; Q8K157; -.
DR PRIDE; Q8K157; -.
DR ProteomicsDB; 267418; -.
DR Antibodypedia; 29513; 223 antibodies from 26 providers.
DR Ensembl; ENSMUST00000039205; ENSMUSP00000040580; ENSMUSG00000035473.
DR GeneID; 319625; -.
DR KEGG; mmu:319625; -.
DR UCSC; uc008dqo.1; mouse.
DR CTD; 130589; -.
DR MGI; MGI:2442420; Galm.
DR VEuPathDB; HostDB:ENSMUSG00000035473; -.
DR eggNOG; KOG1604; Eukaryota.
DR GeneTree; ENSGT00510000047589; -.
DR HOGENOM; CLU_031753_2_0_1; -.
DR InParanoid; Q8K157; -.
DR OMA; ATWLSCK; -.
DR OrthoDB; 978899at2759; -.
DR PhylomeDB; Q8K157; -.
DR TreeFam; TF324207; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00242; -.
DR BioGRID-ORCS; 319625; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Galm; mouse.
DR PRO; PR:Q8K157; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K157; protein.
DR Bgee; ENSMUSG00000035473; Expressed in olfactory epithelium and 223 other tissues.
DR ExpressionAtlas; Q8K157; baseline and differential.
DR Genevisible; Q8K157; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004034; F:aldose 1-epimerase activity; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; ISO:MGI.
DR GO; GO:0006012; P:galactose metabolic process; ISO:MGI.
DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR018052; Ald1_epimerase_CS.
DR InterPro; IPR015443; Aldose_1-epimerase.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF005096; GALM; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT CHAIN 2..342
FT /note="Galactose mutarotase"
FT /id="PRO_0000197434"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 81..82
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 107
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 176..178
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 243
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 279
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 307
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
SQ SEQUENCE 342 AA; 37799 MW; EEF74211B6F3426B CRC64;
MVSVTRTVFG ELPSGGGTVE KFQLRSDQLS VDIISWGCTI TALQVKDRQG KASDVVLGFA
ELEGYLQKQP YFGAVVGRVA NRIAKGRFTI GGKEYHLPVN REPNSLHGGF TGFDKVLWTP
QVLTNGVQFF RVSPDGEEGY PGELKVWVTY TLDGGELVIN YRAQASQTTP VNLTNHSYFN
LAGQGSPNIY DHEVTIAADA YLPVDETLIP TGVIAPVEGT AFDLRKPVEL GTHLQDYHIH
GFDHNFCLKE SKEKKFCARV RHAASGRILE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK
HSGLCLETQN WPDSVNQPQF PPALLRPGEE YNHTTWFKFS VA
