GALM_PIG
ID GALM_PIG Reviewed; 342 AA.
AC Q9GKX6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Kitazawa S., Mori H., Kato N., Ono C., Ito H., Kimura A., Matsui H.,
RA Chiba S.;
RT "Molecular cloning of an aldose 1-epimerase (mutarotase) cDNA from hog
RT kidney and its overexpression in Escherichia coli and some properties of
RT recombinant enzyme.";
RL Submitted (JUN-2000) 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; AB044390; BAB18973.1; -; mRNA.
DR RefSeq; NP_999571.1; NM_214406.1.
DR AlphaFoldDB; Q9GKX6; -.
DR SMR; Q9GKX6; -.
DR STRING; 9823.ENSSSCP00000009052; -.
DR PaxDb; Q9GKX6; -.
DR PeptideAtlas; Q9GKX6; -.
DR PRIDE; Q9GKX6; -.
DR Ensembl; ENSSSCT00070009543; ENSSSCP00070007827; ENSSSCG00070005030.
DR GeneID; 399536; -.
DR KEGG; ssc:399536; -.
DR CTD; 130589; -.
DR eggNOG; KOG1604; Eukaryota.
DR HOGENOM; CLU_031753_2_0_1; -.
DR InParanoid; Q9GKX6; -.
DR OMA; ATWLSCK; -.
DR OrthoDB; 978899at2759; -.
DR TreeFam; TF324207; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 3.
DR Genevisible; Q9GKX6; SS.
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_0000197435"
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"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HG4"
SQ SEQUENCE 342 AA; 37816 MW; C824C57AC488E3D2 CRC64;
MVSVTRSVFG DLPSGAGTVE KFQLQSDQLR VDIISWGCTI TALEVKDRQG RASDVVLGFA
ELKEYLQKHP YFGAVVGRVA NRIAKGTFTL DGKEYKLAIN NGPNSLHGGV RGFDKVLWTP
RVLSNGIEFS RVSPDGEEGY PGELKVWVTY TLDGGELVVN YRAQASQTTP VNLTNHSYFN
LAGQGSPNIY DHEVTIEADA FLPVDETLIP TGEIAPVQGT AFDLRKPVEL GKHLQEFHIN
GFDHNFCLKR SKEKQFCARV HHAGSGRVLE VYTTQPGIQF YTGNFLDGTL KGKTGAVYPK
HSGFCLETQN WPNAVNQPHF PPVLLKPGEE YNHTTWFVFS VA
