ID   LSRE_SALCH              Reviewed;         254 AA.
AC   Q57HD7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Putative epimerase LsrE;
DE            EC=5.1.3.- {ECO:0000250|UniProtKB:P32719};
GN   Name=lsrE; OrderedLocusNames=SCH_3969;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P32719};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:P32719};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000305}.
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; AE017220; AAX67875.1; -; Genomic_DNA.
DR   RefSeq; WP_001088049.1; NC_006905.1.
DR   AlphaFoldDB; Q57HD7; -.
DR   SMR; Q57HD7; -.
DR   EnsemblBacteria; AAX67875; AAX67875; SCH_3969.
DR   KEGG; sec:SCH_3969; -.
DR   HOGENOM; CLU_054856_3_0_6; -.
DR   OMA; GQFSPFF; -.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00429; RPE; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000056; Ribul_P_3_epim-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR11749; PTHR11749; 1.
DR   Pfam; PF00834; Ribul_P_3_epim; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Isomerase; Membrane; Metal-binding; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="Putative epimerase LsrE"
FT                   /id="PRO_0000351557"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        52
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         50
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         52
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         81
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         166..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         199..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         199
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         221..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
SQ   SEQUENCE   254 AA;  27635 MW;  F8272A0A05F15451 CRC64;
     MNSQFAGLTR EACVALLASY PLSVGILAGQ WIALHRYLQQ LEALNQPLLH LDLMDGQFCP
     QFTVGPWAVG QLPQTFIKDV HLMVADQWTA AQACVKAGAH CITLQAEGDI HLHHTLSWLG
     QQTVPVIGGE MPVIRGISLC PATPLDVIIP ILSDVEVIQL LAVNPGYGSK MRSSDLHERV
     AQLLCLLGDK REGKIIVIDG SLTQDQLPSL IAQGIDRVVS GSALFRDDRL VENTRSWRAM
     FKVAGDTTFL PSTA