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Database: UniProt
Entry: A0A1S3SAW8_SALSA
LinkDB: A0A1S3SAW8_SALSA
Original site: A0A1S3SAW8_SALSA 
ID   A0A1S3SAW8_SALSA        Unreviewed;       344 AA.
AC   A0A1S3SAW8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   Name=galm {ECO:0000313|RefSeq:XP_014061477.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014061477.1};
RN   [1] {ECO:0000313|RefSeq:XP_014061477.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014061477.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Mutarotase that catalyzes the interconversion of beta-D-
CC       galactose and alpha-D-galactose during galactose metabolism.
CC       {ECO:0000256|PIRNR:PIRNR005096}.
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:0000256|ARBA:ARBA00001712};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28677;
CC         Evidence={ECO:0000256|ARBA:ARBA00001712};
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:0000256|ARBA:ARBA00001614,
CC         ECO:0000256|PIRNR:PIRNR005096};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC       ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR   RefSeq; XP_014061477.1; XM_014206002.1.
DR   AlphaFoldDB; A0A1S3SAW8; -.
DR   STRING; 8030.ENSSSAP00000098735; -.
DR   PaxDb; 8030-ENSSSAP00000098735; -.
DR   Ensembl; ENSSSAT00000209874; ENSSSAP00000121773; ENSSSAG00000073948.
DR   GeneID; 106608200; -.
DR   KEGG; sasa:106608200; -.
DR   CTD; 130589; -.
DR   OMA; AFCCEPG; -.
DR   OrthoDB; 118242at2759; -.
DR   UniPathway; UPA00214; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000087266; Chromosome ssa01.
DR   Bgee; ENSSSAG00000073948; Expressed in actinopterygian pyloric caecum and 15 other cell types or tissues.
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   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         80..81
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         175..177
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         242
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   344 AA;  37516 MW;  0F1F27F5482CCD5E CRC64;
     MALVLMEEFG EVPGEGRVQK WILKSSNITV EIITLGCIIT AIKCKGKNGE VNDIVLGYDD
     LEGYLANPKY FGAVVGRVAN RIAKGRFVVD GKDYQLAINN GPNSLHGGLR GFSKVIWGSE
     GVEGGVRLTL TSPDGDQNYP GEVQASVTYT LEGDTLSIQY QARSTRTTPI NLTNHSYFNL
     AGQGSADIYD HEVSINAPTY LPVDDVMIPT GEVRPVEHTP FDLRRPVLIG PRLKEVPGPG
     FDHNFCLSSP GDAWTVRVCA RVFHPASGRV VEVSTTQPGV QFYTANFLDG SFKGKGGASY
     PKHSAFCLET QNWPDAVNQA SFPDALLRPG EQYRHVTRFT FSTT
//
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