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Database: UniProt
Entry: B3RSA1_TRIAD
LinkDB: B3RSA1_TRIAD
Original site: B3RSA1_TRIAD 
ID   B3RSA1_TRIAD            Unreviewed;       277 AA.
AC   B3RSA1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE            EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN   ORFNames=TRIADDRAFT_54524 {ECO:0000313|EMBL:EDV27019.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV27019.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV27019.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV27019.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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 6-phosphate = beta-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC         EC=5.1.3.15; Evidence={ECO:0000256|ARBA:ARBA00001096};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00005866, ECO:0000256|PIRNR:PIRNR016020}.
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DR   EMBL; DS985243; EDV27019.1; -; Genomic_DNA.
DR   RefSeq; XP_002111015.1; XM_002110979.1.
DR   AlphaFoldDB; B3RSA1; -.
DR   STRING; 10228.B3RSA1; -.
DR   EnsemblMetazoa; TriadT54524; TriadP54524; TriadG54524.
DR   GeneID; 6751691; -.
DR   KEGG; tad:TRIADDRAFT_54524; -.
DR   CTD; 6751691; -.
DR   eggNOG; KOG1594; Eukaryota.
DR   HOGENOM; CLU_048345_1_0_1; -.
DR   InParanoid; B3RSA1; -.
DR   OMA; TQALHSY; -.
DR   OrthoDB; 915361at2759; -.
DR   PhylomeDB; B3RSA1; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IBA:GO_Central.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09020; D-hex-6-P-epi_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR025532; G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR11122; APOSPORY-ASSOCIATED PROTEIN C-RELATED; 1.
DR   PANTHER; PTHR11122:SF39; GLUCOSE-6-PHOSPHATE 1-EPIMERASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PIRNR:PIRNR016020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ   SEQUENCE   277 AA;  31514 MW;  8F4856E994D54EF4 CRC64;
     MAAADDVVEL NLDQENICKV NLHGATLTSW LCDGTEMLFV SQQAVFNNVK AIRGGIPIVY
     PHFGPWELGP QHGFARISRW TLEKPPAKDG DTVSATFLLQ DNENTRQMWQ DNRFNLFYTV
     IIGKRQLKLK LDVRNEGNDS FEFTTLLHTY FKTLDVNKVT ISGLKSLKYI DKVRQSKKFV
     EENDLVTVKE FVDRLYIGSV DRNEVTNLNG NQNVVMTRVN LPDVVVWNPW QEKAKVMSDF
     GDEEYKEMIC VEAGYVAKPR SLSAGARFEA SVVLDVI
//
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