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Database: UniProt
Entry: I0GM69_SELRL
LinkDB: I0GM69_SELRL
Original site: I0GM69_SELRL 
ID   I0GM69_SELRL            Unreviewed;       375 AA.
AC   I0GM69;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=SELR_01480 {ECO:0000313|EMBL:BAL81856.1};
OS   Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL81856.1, ECO:0000313|Proteomes:UP000007887};
RN   [1] {ECO:0000313|EMBL:BAL81856.1, ECO:0000313|Proteomes:UP000007887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA   Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA   Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT   TAM6421.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP012292; BAL81856.1; -; Genomic_DNA.
DR   RefSeq; WP_014423303.1; NC_017068.1.
DR   AlphaFoldDB; I0GM69; -.
DR   KEGG; sri:SELR_01480; -.
DR   PATRIC; fig|927704.6.peg.152; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_2_0_9; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000007887; 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        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        339
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         81..82
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         180..182
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         252
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   375 AA;  41847 MW;  A199CBCF7EC1B91D CRC64;
     MATVKQESFG KLSDGQEVFL YTLRNTKGTE VKITNYGARL VSWRVFGKDA KKIDILLGYA
     DAAAYEKDDT SMGGLVGRHA NRIAGGKAVI NGQEYQLDLN DGSRMQNHIH GGSKGFHNEL
     WQAEEIYEGI KLTYHSKDGD GGYPGNMDVT VIYSLSNDNE LSIKYEAVSD KDTICNLTNH
     SYFNLDGFAS PSILDQKIQI FADQYTWADS ESLPDGRILP VEGTPMDLRQ PVRIGEHIDD
     DFDELVMGKG YDHNWVLRDE PVHVEMKPGM FGYDPHCPID YQKRGLKKAA YAESDQSGLT
     LTCYTTLPGV QFYTGNFLDG SLPGKDGVTF PRRSGFCLET QYFPNSLANP AFPQPVIKAG
     EKWEAQTIFV LFPKD
//
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