ID   E0RNV6_SPITD            Unreviewed;       375 AA.
AC   E0RNV6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN   OrderedLocusNames=STHERM_c02560 {ECO:0000313|EMBL:ADN01229.1};
OS   Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=665571 {ECO:0000313|EMBL:ADN01229.1, ECO:0000313|Proteomes:UP000001296};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 6192;
RA   Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H., Daniel R.,
RA   Liebl W.;
RT   "The genome sequence of Spirochaeta thermophila DSM6192.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADN01229.1, ECO:0000313|Proteomes:UP000001296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1
RC   {ECO:0000313|Proteomes:UP000001296};
RX   PubMed=20935097; DOI=10.1128/JB.01023-10;
RA   Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R., Liesegang H.,
RA   Daniel R., Liebl W.;
RT   "Genome sequence of the polysaccharide-degrading, thermophilic anaerobe
RT   Spirochaeta thermophila DSM 6192.";
RL   J. Bacteriol. 192:6492-6493(2010).
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; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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}.
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; CP001698; ADN01229.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0RNV6; -.
DR   PaxDb; 665571-STHERM_c02560; -.
DR   KEGG; sta:STHERM_c02560; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_2_0_12; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001296; Chromosome.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0019318; P:hexose 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}.
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         112..113
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         212..214
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         278
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   375 AA;  41778 MW;  AC0B89012684823E CRC64;
     MHDNSVEYSS PLCNGGWGDM IYGARKRSRR RSMQVDKKTF GTTRDGREVY AYTLDTEKGF
     SCTVISYGAT LLSFRMPDRE GRVGEITCGF DSLSDYEERN PYFGSTIGRF ANRIGGARFV
     LDGVEYRLVA NEGANQLHGG PGGFHAVVWE SEAFSREDAA TVVLSYRSPD GDQGFPGNLE
     VTASYTLTEE GHLILEYAAE TDRPTPVNLT NHAYWNLSGP GSGLVLDHLL TLRASYYLEV
     DEGLIPTGRM IPVEGTPFDF REEKPIGRDF DEVKGGYDHC FVVDGEGFRQ VAVVREPSTG
     RRMEVWSTKP GVQFYTGNHL NDIEIAGGVT VPSYGAFCLE TQYFPDSPNK PVFPPCILRP
     GETYRHRTEL RFSVE
//