ID   LSRE_SALPA              Reviewed;         254 AA.
AC   Q5PJE1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative epimerase LsrE;
DE            EC=5.1.3.- {ECO:0000250|UniProtKB:P32719};
GN   Name=lsrE; OrderedLocusNames=SPA3923;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
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DR   EMBL; CP000026; AAV79688.1; -; Genomic_DNA.
DR   RefSeq; WP_001088041.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJE1; -.
DR   SMR; Q5PJE1; -.
DR   EnsemblBacteria; AAV79688; AAV79688; SPA3923.
DR   KEGG; spt:SPA3923; -.
DR   HOGENOM; CLU_054856_3_0_6; -.
DR   OMA; GQFSPFF; -.
DR   Proteomes; UP000008185; 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_0000351558"
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;  27679 MW;  08222B696493544B CRC64;
     MNSQFAGLTR EACVALLASY PLSVGILAGQ WIALHRYLQQ LEALNQPLLH LDLMDGQFCP
     QFTVGPWAVE QLPQTFIKDV HLMVADQWTA AQACVKAGAH CITLQAEGDI HLHHTLSWLG
     QQTVPVIGGE MPVIRGISLC PATPLDVIIP ILSDVEVIQL LAVNPGYGSK MRSSDLHERV
     AQLLCLLGDK REGKIIVIDG SLTQDQLPSL IAQGIDRVVS GSALFRDDRL AENTRSWRAM
     FKVAGDTTFL PSTA