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Database: UniProt
Entry: B7MGL3_ECO45
LinkDB: B7MGL3_ECO45
Original site: B7MGL3_ECO45 
ID   B7MGL3_ECO45            Unreviewed;       346 AA.
AC   B7MGL3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00014165, ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN   Name=galM {ECO:0000313|EMBL:CAR02111.1};
GN   OrderedLocusNames=ECS88_0772 {ECO:0000313|EMBL:CAR02111.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR02111.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR   EMBL; CU928161; CAR02111.1; -; Genomic_DNA.
DR   RefSeq; WP_000931396.1; NC_011742.1.
DR   AlphaFoldDB; B7MGL3; -.
DR   SMR; B7MGL3; -.
DR   KEGG; ecz:ECS88_0772; -.
DR   HOGENOM; CLU_031753_1_0_6; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000747; 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:0006012; P:galactose metabolic process; IEA:InterPro.
DR   CDD; cd09019; galactose_mutarotase_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR013458; Ald_epimerase_bac.
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   NCBIfam; TIGR02636; galM_Leloir; 1.
DR   PANTHER; PTHR10091:SF50; ALDOSE 1-EPIMERASE; 1.
DR   PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         78..79
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         175..177
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         245
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   346 AA;  38231 MW;  EF527FDAA3B9F57D CRC64;
     MLNETPALAP DGQPYRLLTL RNNAGMVVTL MDWGATLLSA RIPLSDGSVR EALLGCASPE
     CYQDQAAFLG ASIGRYANRI ANSRYTFDGE TVTLSPSQGV NQLHGGPEGF DKRRWQIVNQ
     NDRQVLFALS SDDGDQGFPG NLGATVQYRL TDDNRISITY RATVDKPCPV NMTNHVYFNL
     DGEQSDVRNH KLQILAEEYL PVDEGGIPHD GLKSVAGTSF DFRNAKIIAS EFLADDDQRK
     VKGYDHAFLL QAKGDGKKVA AHVWSADEKL QLKVYTTAPA LQFYSGNFLG GTPSRGTEPY
     ADWQGLALES EFLPDSPNHP EWPQPDCFLR PGEEYSSLTE YQFIAQ
//
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