ID   GALM_RAT                Reviewed;         342 AA.
AC   Q66HG4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Galactose mutarotase;
DE            EC=5.1.3.3 {ECO:0000250|UniProtKB:Q96C23};
DE   AltName: Full=Aldose 1-epimerase;
GN   Name=Galm;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [2]
RP   PROTEIN SEQUENCE OF 69-78 AND 146-162, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-124, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC081876; AAH81876.1; -; mRNA.
DR   RefSeq; NP_001007705.1; NM_001007704.1.
DR   AlphaFoldDB; Q66HG4; -.
DR   SMR; Q66HG4; -.
DR   STRING; 10116.ENSRNOP00000009221; -.
DR   iPTMnet; Q66HG4; -.
DR   PhosphoSitePlus; Q66HG4; -.
DR   PaxDb; Q66HG4; -.
DR   PRIDE; Q66HG4; -.
DR   GeneID; 313843; -.
DR   KEGG; rno:313843; -.
DR   UCSC; RGD:1359459; rat.
DR   CTD; 130589; -.
DR   RGD; 1359459; Galm.
DR   VEuPathDB; HostDB:ENSRNOG00000007023; -.
DR   eggNOG; KOG1604; Eukaryota.
DR   HOGENOM; CLU_031753_2_0_1; -.
DR   InParanoid; Q66HG4; -.
DR   OMA; GPAVNWA; -.
DR   OrthoDB; 978899at2759; -.
DR   PhylomeDB; Q66HG4; -.
DR   TreeFam; TF324207; -.
DR   UniPathway; UPA00214; -.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:Q66HG4; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000007023; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q66HG4; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; ISO:RGD.
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:RGD.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR   GO; GO:0006012; P:galactose metabolic process; ISO:RGD.
DR   GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
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; Direct protein sequencing; Isomerase;
KW   Phosphoprotein; 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_0000197437"
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:0007744|PubMed:22673903"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   342 AA;  37893 MW;  2168267DCA6D44C3 CRC64;
     MVSVTRTVFG ELPSGGGAVE KFQLRSDQLN VDIISWGCTI TALQVKDRQG KASDVVLGFA
     ELEGYLQKQP YFGAVVGRVA NRIAKGRFTV DGKEYHLPIN REPNSLHGGF RGFDKVLWTP
     QVLSNGVQFS RVSPDGEEGY PGELKVWVTY TLDGGELVVN YRAQASQTTP VNLTNHSYFN
     LAGQGSPDIY DHEVTIAADA YLPVDETLIP TGVIAPVEGT AFDLRKPVEL GKHLQSYHIH
     GFDHNFCLKE SKEKKFCARV HHAASGRILE VYTTQPGVQF YTGNFLDGTL KGKSGEVYPK
     HSGFCLETQN WPDAVNQPQF PPILLRPGEE YNHTTWFKFS VA