ID   FRLC_ECO57              Reviewed;         275 AA.
AC   Q8X840;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Fructoselysine 3-epimerase {ECO:0000250|UniProtKB:P45541};
DE            EC=5.1.3.41 {ECO:0000250|UniProtKB:P45541};
GN   Name=frlC; OrderedLocusNames=Z4733, ECs4223;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of fructoselysine
CC       with its C-3 epimer, psicoselysine. Allows E.coli to utilize
CC       psicoselysine for growth. Does not act on psicose or fructoselysine 6-
CC       phosphate. {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=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000250|UniProtKB:P45541};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:P45541};
CC       Note=Can use Ni(2+) or Co(2+) in vitro, and, to a lesser extent, Fe(2+)
CC       or Mn(2+), but not Ca(2+) or Cu(2+). {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; AE005174; AAG58480.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37646.1; -; Genomic_DNA.
DR   PIR; D86002; D86002.
DR   PIR; G91156; G91156.
DR   RefSeq; NP_312250.1; NC_002695.1.
DR   RefSeq; WP_000847833.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X840; -.
DR   SMR; Q8X840; -.
DR   STRING; 155864.EDL933_4578; -.
DR   EnsemblBacteria; AAG58480; AAG58480; Z4733.
DR   EnsemblBacteria; BAB37646; BAB37646; ECs_4223.
DR   GeneID; 915922; -.
DR   KEGG; ece:Z4733; -.
DR   KEGG; ecs:ECs_4223; -.
DR   PATRIC; fig|386585.9.peg.4408; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_050006_5_1_6; -.
DR   OMA; TRHIHIE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   Cobalt; Isomerase; Metal-binding; Nickel; Reference proteome.
FT   CHAIN           1..275
FT                   /note="Fructoselysine 3-epimerase"
FT                   /id="PRO_0000087337"
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   275 AA;  30999 MW;  332AC8C4F945EBB9 CRC64;
     MKTGMFTCGH QRLPIEHAFR DASELGYDGI EIWGGRPHAF APDLKAGGIK QIKALAQTYQ
     MPIIGYTPET NGYPYNMMLG DEHMRRESLD MIKLAMDMAK EMNAGYTLIS AAHAGYLTPP
     NVIWGRLAEN LSELCEYAEN IGMDLILEPL TPYESNVVCN ANDVLHALAL VPSPRLFSMV
     DICAPYVQAE PVMSYFDKLG DKLRHLHIVD SDGASDTHYI PGEGKMPLRE LMRDIIDRGY
     EGYCTVELVT MYMNEPRLYA RQALERFRAL LPEDE