GALM_PONAB
ID GALM_PONAB Reviewed; 342 AA.
AC Q5R8U1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859658; CAH91819.1; -; mRNA.
DR RefSeq; NP_001126052.1; NM_001132580.1.
DR AlphaFoldDB; Q5R8U1; -.
DR SMR; Q5R8U1; -.
DR STRING; 9601.ENSPPYP00000013940; -.
DR GeneID; 100173004; -.
DR KEGG; pon:100173004; -.
DR CTD; 130589; -.
DR eggNOG; KOG1604; Eukaryota.
DR InParanoid; Q5R8U1; -.
DR OrthoDB; 978899at2759; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
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 Acetylation; 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_0000197436"
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 2
FT /note="N-acetylalanine"
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; 37819 MW; D00C2A67753D6DFF CRC64;
MASATRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RSSDVVLGFA
ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP
RVLSNGIQFS RISPDGEEGY PGELKVWVTY TLDGGELVVN YRAQASQATP VNLTNHSYFN
LAGQGSPNIY DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN
GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YMGNFLDGTL KGKNGAVYPK
HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA
