ID E3TGI9_ICTPU Unreviewed; 353 AA.
AC E3TGI9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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|EMBL:ADO29425.1};
GN Synonyms=galm {ECO:0000313|RefSeq:NP_001188007.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:ADO29425.1};
RN [1] {ECO:0000313|EMBL:ADO29425.1, ECO:0000313|RefSeq:NP_001188007.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20634964; DOI=10.1371/journal.pone.0011546;
RA Chen F., Lee Y., Jiang Y., Wang S., Peatman E., Abernathy J., Liu H.,
RA Liu S., Kucuktas H., Ke C., Liu Z.;
RT "Identification and characterization of full-length cDNAs in channel
RT catfish (Ictalurus punctatus) and blue catfish (Ictalurus furcatus).";
RL PLoS ONE 5:E11546-E11546(2010).
RN [2] {ECO:0000313|RefSeq:NP_001188007.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27307075;
RA Zeng Q., Liu S., Yao J., Zhang Y., Yuan Z., Jiang C., Chen A., Fu Q.,
RA Su B., Dunham R., Liu Z.;
RT "Transcriptome Display During Testicular Differentiation of Channel Catfish
RT (Ictalurus punctatus) as Revealed by RNA-Seq Analysis.";
RL Biol. Reprod. 95:19-19(2016).
RN [3] {ECO:0000313|RefSeq:NP_001188007.1}
RP IDENTIFICATION.
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 EMBL; GU589475; ADO29425.1; -; mRNA.
DR RefSeq; NP_001188007.1; NM_001201078.1.
DR STRING; 7998.ENSIPUP00000003623; -.
DR Ensembl; ENSIPUT00000003830; ENSIPUP00000003652; ENSIPUG00000002550.
DR GeneID; 100528808; -.
DR KEGG; ipu:100528808; -.
DR CTD; 130589; -.
DR OMA; AFCCEPG; -.
DR OrthoDB; 118242at2759; -.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000221080; Chromosome 3.
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 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}.
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 353 AA; 38793 MW; 17822D89A3C8EBD0 CRC64;
MSEVKKDVLA LVSGQRSVEK WTLRSKSVSV EIISLGCVIA AIRTLDRKGQ SADIVLGFGD
LESYLTNSRY FGAVVGRVAN RIAKGQFVIE GKVYNLAINN GPNSLHGGIR GFDKAVWSCE
PVPNGVRLSH MSPNGDEGYP GNLKVSVTYT LEENTLSVQY CAQTDQTTPI NLTNHSYFNL
AGQGAPDIYD HEVSISAEAY LPVDDNMIPT GEIRPVENSL FDLRKSVLLG SRLKELPGPG
FDHNFCLWLP GQHKQEMKCA RVVHPGTGRV LELSTTQPGV QFYTSNFLDG TVGGKEGTSY
PKHSAFCLET QNWPDAVNQP QFPEALLRPG EEYTHTTRFT FSVVSDINIH KTD
//
