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Database: UniProt
Entry: R9MBW7_9FIRM
LinkDB: R9MBW7_9FIRM
Original site: R9MBW7_9FIRM 
ID   R9MBW7_9FIRM            Unreviewed;       337 AA.
AC   R9MBW7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=C816_02123 {ECO:0000313|EMBL:EOS65342.1};
OS   Oscillibacter sp. 1-3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillibacter.
OX   NCBI_TaxID=1235797 {ECO:0000313|EMBL:EOS65342.1, ECO:0000313|Proteomes:UP000014108};
RN   [1] {ECO:0000313|EMBL:EOS65342.1, ECO:0000313|Proteomes:UP000014108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-3 {ECO:0000313|EMBL:EOS65342.1,
RC   ECO:0000313|Proteomes:UP000014108};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Oscillibacter bacterium 1-3.";
RL   Submitted (APR-2013) 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|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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOS65342.1}.
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DR   EMBL; ASTC01000015; EOS65342.1; -; Genomic_DNA.
DR   RefSeq; WP_016322412.1; NZ_KE159708.1.
DR   AlphaFoldDB; R9MBW7; -.
DR   STRING; 1235797.C816_02123; -.
DR   PATRIC; fig|1235797.3.peg.2342; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_2_0_9; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000014108; Unassembled WGS sequence.
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; 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.
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:UP000014108}.
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        302
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         77..78
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         172..174
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   337 AA;  36052 MW;  B007761DFE1A192E CRC64;
     MVTQEIFGRL DGREIPLLTL TEGPVSVELI PLGAAVRAIR VPDRKGRTVD VCLGYDTPAE
     YRDWNSALGG TLGRCANRIG GARFAIGGAE YRLTANEGAN TLHGGAEGFH KKLWSCAVEE
     HSAAFFLDSP DGEEGFPGNL HAEVTYTLQN GVLTMEYRAS CDRDTVVNLS NHTYFNLAGH
     DAGSIAGHRV TLGAGRYTPS GAGNVPTGEI APVDGTPLDL RQGALLEERL GDPFLAATRG
     YDHNFVLDGG GLAAEVCCPA TGIALEVRTT LEGMQFYTSG FLTDRPGKSG ARYGRASGLC
     LETQRFPDAV NHPSFPSPVL RAGEAYREAT SWRFFVK
//
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