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 27-MAR-2024, 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 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}.
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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; 9913-ENSBTAP00000028111; -.
DR PeptideAtlas; Q5EA79; -.
DR Ensembl; ENSBTAT00000028111.4; ENSBTAP00000028111.3; ENSBTAG00000021102.4.
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; AFCCEPG; -.
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 cell types or 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 CDD; cd09019; galactose_mutarotase_like; 1.
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; IPR047215; Galactose_mutarotase-like.
DR InterPro; IPR014718; GH-type_carb-bd.
DR PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1.
DR PANTHER; PTHR10091:SF0; GALACTOSE MUTAROTASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF005096; GALM; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 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
//
