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Database: UniProt
Entry: U2MV69_9BACT
LinkDB: U2MV69_9BACT
Original site: U2MV69_9BACT 
ID   U2MV69_9BACT            Unreviewed;       362 AA.
AC   U2MV69;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=HMPREF9145_2649 {ECO:0000313|EMBL:ERK03099.1};
OS   Segatella salivae F0493.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=1395125 {ECO:0000313|EMBL:ERK03099.1, ECO:0000313|Proteomes:UP000017023};
RN   [1] {ECO:0000313|EMBL:ERK03099.1, ECO:0000313|Proteomes:UP000017023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0493 {ECO:0000313|EMBL:ERK03099.1,
RC   ECO:0000313|Proteomes:UP000017023};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:ERK03099.1}.
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DR   EMBL; AWGW01000002; ERK03099.1; -; Genomic_DNA.
DR   RefSeq; WP_021824329.1; NZ_AWGW01000002.1.
DR   AlphaFoldDB; U2MV69; -.
DR   GeneID; 78496781; -.
DR   PATRIC; fig|1395125.3.peg.18; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000017023; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         90..91
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         261
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   362 AA;  40469 MW;  1E0459038909D3C2 CRC64;
     MNTVPNENIC GLKREDFQTT VNGKKTDLYI LRNALGNEVA ITNYGGAVVA IMVPDREGNY
     ANVIQGHDNI NDVINSPEPY LSRLIGRFGN RIAKGRFQLH GKEYCLPINN GPNSLHGGKK
     GFNDKVWDAE LMNEQALVLH YVSSYGEEGF SGELKTTVVY TFNDDNELVI DYLACTNKKT
     IINLTHHAFF SLAGIANPTP TIDTLECELN ADFYIPIDET SIPTGEILKV EGTPFDFRKP
     QAIGKRINDD NEQIKNGSGY DHCFVLNKKE EGELSFAAKI VEPHSGRTME MYTTEPGVQM
     YTGNFENGMK GTHGATYPRR SAVCFEAEHF PDTPNRPYFP SVVLNPGEQY KQKTIYKFGI
     DK
//
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