ID   GALM_BOVIN              Reviewed;         342 AA.
AC   Q5EA79; Q3T0D4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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; BT020690; AAX08707.1; -; mRNA.
DR   EMBL; BC102446; AAI02447.1; -; mRNA.
DR   RefSeq; NP_001029967.1; NM_001034795.1.
DR   AlphaFoldDB; Q5EA79; -.
DR   SMR; Q5EA79; -.
DR   STRING; 9913.ENSBTAP00000028111; -.
DR   PaxDb; Q5EA79; -.
DR   PeptideAtlas; Q5EA79; -.
DR   PRIDE; Q5EA79; -.
DR   Ensembl; ENSBTAT00000028111; ENSBTAP00000028111; ENSBTAG00000021102.
DR   GeneID; 616676; -.
DR   KEGG; bta:616676; -.
DR   CTD; 130589; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021102; -.
DR   VGNC; VGNC:29221; GALM.
DR   eggNOG; KOG1604; Eukaryota.
DR   GeneTree; ENSGT00510000047589; -.
DR   HOGENOM; CLU_031753_2_0_1; -.
DR   InParanoid; Q5EA79; -.
DR   OMA; ATWLSCK; -.
DR   OrthoDB; 978899at2759; -.
DR   TreeFam; TF324207; -.
DR   UniPathway; UPA00214; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000021102; Expressed in cortex of kidney and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
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   2: Evidence at transcript 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_0000197432"
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         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66HG4"
SQ   SEQUENCE   342 AA;  37614 MW;  965625452741CDD4 CRC64;
     MVSVTRAVFG DLPLGAGTVE KFQLQSDQLR VDIISWGCTI TALEVKDRQG RASDVVLGFD
     ELEGYLQKQP YFGAVVGRVA NRIAKGTFTL DGKEYKLAIN NGPNSLHGGV KGFDKVLWTP
     RVLSNGVEFS RVSPDGEEGY PGELKVWVMY TLDGGELVVN YRAQASQTTP VNLTNHSYFN
     LAGQGSPNIY DHEVTIEADA FLPVDEVLIP TGEIASVQGT AFDLRKPVEL GKHLQEFHVN
     GFDHNFCLKG SKEKRFCARV HHAGSGRVLE VYTTQPGVQF YTGNFLDGTL KGKSGAGYPK
     HSGFCLETQS WPDAVNQPHF PPVLLKPGEE YDHTTWFKFS VA