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-MAY-2023, entry version 77. 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}. 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; 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; 118242at2759; -. 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 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 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 //