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FRLC_SHIFL
ID   FRLC_SHIFL              Reviewed;         276 AA.
AC   Q83JB2; Q7UAR9;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Fructoselysine 3-epimerase {ECO:0000250|UniProtKB:P45541};
DE            EC=5.1.3.41 {ECO:0000250|UniProtKB:P45541};
GN   Name=frlC; OrderedLocusNames=SF3391, S4371;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of fructoselysine
CC       with its C-3 epimer, psicoselysine. May allow S.flexneri to utilize
CC       psicoselysine for growth. {ECO:0000250|UniProtKB:P45541}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(D-psicosyl)-L-lysine = N(6)-(D-fructosyl)-L-lysine;
CC         Xref=Rhea:RHEA:28390, ChEBI:CHEBI:61393, ChEBI:CHEBI:61403;
CC         EC=5.1.3.41; Evidence={ECO:0000250|UniProtKB:P45541};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P45541};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:P45541}.
CC   -!- SIMILARITY: Belongs to the FrlC family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN44853.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19325.1; -; Genomic_DNA.
DR   RefSeq; NP_709146.2; NC_004337.2.
DR   RefSeq; WP_000847821.1; NZ_WPGW01000003.1.
DR   AlphaFoldDB; Q83JB2; -.
DR   SMR; Q83JB2; -.
DR   STRING; 198214.SF3391; -.
DR   EnsemblBacteria; AAN44853; AAN44853; SF3391.
DR   EnsemblBacteria; AAP19325; AAP19325; S4371.
DR   GeneID; 1026517; -.
DR   KEGG; sfl:SF3391; -.
DR   KEGG; sft:NCTC1_03672; -.
DR   KEGG; sfx:S4371; -.
DR   PATRIC; fig|198214.7.peg.4004; -.
DR   HOGENOM; CLU_050006_5_1_6; -.
DR   OMA; TRHIHIE; -.
DR   OrthoDB; 1007505at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
PE   3: Inferred from homology;
KW   Isomerase; Metal-binding; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Fructoselysine 3-epimerase"
FT                   /id="PRO_0000087339"
FT   ACT_SITE        148
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   ACT_SITE        247
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   BINDING         148
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   BINDING         181
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   BINDING         207
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
SQ   SEQUENCE   276 AA;  31121 MW;  751681CCC7E22B45 CRC64;
     MKTGMFTCGH QRLPIEHAFR DASELGYDGI EIWGGRPHAF APDLKAGGIK QIKALAQTYQ
     MPIIGYTPET NGYPYNMMLG DEHMRRESLD MIKLAIDMAK EMNAGYTLIS AAHAGYLTPP
     NVIWGRLAEN LSELCEYAEN IGMDLILEPL TPYESNVVCN ANDVLHALAL VPSPRLFSMV
     DICAPYVQAE PVMSYFDKLG DKLRHLHIVD SDGASDTHYI PGEGKMPLRE LMRDIIDRGY
     EGYSTVELVT MYMNEPRLYA RQALERFRAL LPEDER
 
 
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