ID   LSRE_SALTI              Reviewed;         254 AA.
AC   Q8Z2Y1; Q7C6A4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative epimerase LsrE;
DE            EC=5.1.3.- {ECO:0000250|UniProtKB:P32719};
GN   Name=lsrE; OrderedLocusNames=STY3790, t3538;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO71045.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD09543.1; -; Genomic_DNA.
DR   RefSeq; NP_457972.1; NC_003198.1.
DR   RefSeq; WP_001088043.1; NZ_WSUR01000010.1.
DR   AlphaFoldDB; Q8Z2Y1; -.
DR   SMR; Q8Z2Y1; -.
DR   STRING; 220341.16504659; -.
DR   EnsemblBacteria; AAO71045; AAO71045; t3538.
DR   KEGG; stt:t3538; -.
DR   KEGG; sty:STY3790; -.
DR   PATRIC; fig|220341.7.peg.3868; -.
DR   eggNOG; COG0036; Bacteria.
DR   HOGENOM; CLU_054856_3_0_6; -.
DR   OMA; GQFSPFF; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000351560"
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;  27689 MW;  4D37276B0738F252 CRC64;
     MNSQFAGLTR EACVALLASY PLSVGILAGQ WIALHRYLQQ LEALNQPLLH LDLMDGQFCP
     QFTVGPWAVG QLPQTFIKDV HLMVADQWAA AQACVKAGAH CITLQAEGDI HLHHTLSWLG
     QQTVPVIDGE MPVIRGISLC PATPLDVIIP ILSDVEVIQL LAVNPGYGSK MRSSDLYERV
     AQLLCLLGDK REGKIIVIDG SLTQDQLPSL IAQGIDRVVS GSALFRDDRL VENTRSWRAM
     FKVAGDTTFL PSTA