FRLC_ECOLI
ID FRLC_ECOLI Reviewed; 276 AA.
AC P45541; P45542; Q2M738;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fructoselysine 3-epimerase {ECO:0000303|PubMed:14641112};
DE EC=5.1.3.41 {ECO:0000269|PubMed:14641112};
GN Name=frlC {ECO:0000303|PubMed:12147680}; Synonyms=yhfO, yhfP;
GN OrderedLocusNames=b4474, JW5699;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISCUSSION OF FUNCTION.
RX PubMed=12147680; DOI=10.1074/jbc.m200863200;
RA Wiame E., Delpierre G., Collard F., Van Schaftingen E.;
RT "Identification of a pathway for the utilization of the Amadori product
RT fructoselysine in Escherichia coli.";
RL J. Biol. Chem. 277:42523-42529(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, COFACTOR, ACTIVITY REGULATION, INDUCTION, AND SUBUNIT.
RX PubMed=14641112; DOI=10.1042/bj20031527;
RA Wiame E., Van Schaftingen E.;
RT "Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the
RT unusual Amadori compound psicoselysine in Escherichia coli.";
RL Biochem. J. 378:1047-1052(2004).
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:0000269|PubMed:14641112}.
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:0000269|PubMed:14641112};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:14641112};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:14641112};
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:0000269|PubMed:14641112};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+).
CC {ECO:0000269|PubMed:14641112}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for D-fructosyl-L-lysine {ECO:0000269|PubMed:14641112};
CC Vmax=2.5 umol/min/mg enzyme for the epimerization of D-fructosyl-L-
CC lysine {ECO:0000269|PubMed:14641112};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:14641112}.
CC -!- INDUCTION: Induced by psicoselysine. Makes part of the frl operon with
CC FrlA, FrlB, FrlD and FrlR. {ECO:0000269|PubMed:14641112}.
CC -!- SIMILARITY: Belongs to the FrlC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58169.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA58170.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA58169.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18997; AAA58170.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48177.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77918.1; -; Genomic_DNA.
DR PIR; H65131; H65131.
DR RefSeq; WP_000847837.1; NZ_SSZK01000008.1.
DR RefSeq; YP_026213.1; NC_000913.3.
DR AlphaFoldDB; P45541; -.
DR SMR; P45541; -.
DR BioGRID; 853505; 1.
DR IntAct; P45541; 1.
DR STRING; 511145.b4474; -.
DR PaxDb; P45541; -.
DR PRIDE; P45541; -.
DR EnsemblBacteria; AAT48177; AAT48177; b4474.
DR EnsemblBacteria; BAE77918; BAE77918; BAE77918.
DR GeneID; 2847758; -.
DR KEGG; ecj:JW5699; -.
DR KEGG; eco:b4474; -.
DR PATRIC; fig|1411691.4.peg.3357; -.
DR EchoBASE; EB2747; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_050006_5_1_6; -.
DR InParanoid; P45541; -.
DR OMA; TRHIHIE; -.
DR PhylomeDB; P45541; -.
DR BioCyc; EcoCyc:G7724-MON; -.
DR BioCyc; MetaCyc:G7724-MON; -.
DR PRO; PR:P45541; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0046348; P:amino sugar catabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cobalt; Isomerase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..276
FT /note="Fructoselysine 3-epimerase"
FT /id="PRO_0000087338"
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; 31169 MW; 6C263FC8C4F945EA CRC64;
MKTGMFTCGH QRLPIEHAFR DASELGYDGI EIWGGRPHAF APDLKAGGIK QIKALAQTYQ
MPIIGYTPET NGYPYNMMLG DEHMRRESLD MIKLAMDMAK EMNAGYTLIS AAHAGYLTPP
NVIWGRLAEN LSELCEYAEN IGMDLILEPL TPYESNVVCN ANDVLHALAL VPSPRLFSMV
DICAPYVQAE PVMSYFDKLG DKLRHLHIVD SDGASDTHYI PGEGKMPLRE LMRDIIERGY
EGYCTVELVT MYMNEPRLYA RQALERFRAL LPEDER
