FRLB_ECOLI
ID FRLB_ECOLI Reviewed; 340 AA.
AC P0AC00; P45540; Q2M737;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Fructoselysine 6-phosphate deglycase {ECO:0000303|PubMed:12147680};
DE EC=3.5.-.- {ECO:0000269|PubMed:12147680};
GN Name=frlB {ECO:0000303|PubMed:12147680}; Synonyms=yhfN;
GN OrderedLocusNames=b3371, JW5700;
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 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, PATHWAY, INDUCTION, AND SUBUNIT.
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
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 conversion of fructoselysine 6-
CC phosphate to glucose 6-phosphate and lysine (PubMed:12147680).
CC Functions in a fructoselysine degradation pathway that allows E.coli to
CC grow on fructoselysine or psicoselysine (PubMed:14641112).
CC {ECO:0000269|PubMed:12147680, ECO:0000269|PubMed:14641112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(6-phospho-D-fructosyl)-L-lysine = D-glucose 6-
CC phosphate + L-lysine; Xref=Rhea:RHEA:28382, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:61392, ChEBI:CHEBI:61548;
CC Evidence={ECO:0000269|PubMed:12147680};
CC -!- ACTIVITY REGULATION: Strongly inhibited by ZnCl(2).
CC {ECO:0000269|PubMed:12147680}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for fructoselysine 6-phosphate
CC {ECO:0000269|PubMed:12147680};
CC -!- PATHWAY: Carbohydrate metabolism; fructoselysine degradation; D-glucose
CC 6-phosphate and lysine from fructoselysine: step 2/2.
CC {ECO:0000269|PubMed:14641112, ECO:0000305|PubMed:12147680}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:12147680}.
CC -!- INDUCTION: Induced by fructoselysine and psicoselysine. Makes part of
CC the frl operon with FrlA, FrlC, FrlD and FrlR.
CC {ECO:0000269|PubMed:12147680, ECO:0000269|PubMed:14641112}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC fructoselysine or psicoselysine, where they do grow on glucose.
CC {ECO:0000269|PubMed:14641112}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58168.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U18997; AAA58168.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76396.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77919.1; -; Genomic_DNA.
DR PIR; F65131; F65131.
DR RefSeq; NP_417830.4; NC_000913.3.
DR RefSeq; WP_001295163.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P0AC00; -.
DR SMR; P0AC00; -.
DR BioGRID; 4262480; 197.
DR STRING; 511145.b3371; -.
DR PaxDb; P0AC00; -.
DR PRIDE; P0AC00; -.
DR EnsemblBacteria; AAC76396; AAC76396; b3371.
DR EnsemblBacteria; BAE77919; BAE77919; BAE77919.
DR GeneID; 947875; -.
DR KEGG; ecj:JW5700; -.
DR KEGG; eco:b3371; -.
DR PATRIC; fig|1411691.4.peg.3358; -.
DR EchoBASE; EB2746; -.
DR eggNOG; COG2222; Bacteria.
DR HOGENOM; CLU_012520_3_0_6; -.
DR InParanoid; P0AC00; -.
DR OMA; LMEMQWI; -.
DR PhylomeDB; P0AC00; -.
DR BioCyc; EcoCyc:G7723-MON; -.
DR BioCyc; MetaCyc:G7723-MON; -.
DR SABIO-RK; P0AC00; -.
DR UniPathway; UPA00784; UER00770.
DR PRO; PR:P0AC00; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Repeat.
FT CHAIN 1..340
FT /note="Fructoselysine 6-phosphate deglycase"
FT /id="PRO_0000136593"
FT DOMAIN 35..169
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 201..331
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
SQ SEQUENCE 340 AA; 38569 MW; 503497DD301942C6 CRC64;
MLDIDKSTVD FLVTENMVQE VEKVLSHDVP LVHAIVEEMV KRDIDRIYFV ACGSPLNAAQ
TAKHLADRFS DLQVYAISGW EFCDNTPYRL DDRCAVIGVS DYGKTEEVIK ALELGRACGA
LTAAFTKRAD SPITSAAEFS IDYQADCIWE IHLLLCYSVV LEMITRLAPN AEIGKIKNDL
KQLPNALGHL VRTWEEKGRQ LGELASQWPM IYTVAAGPLR PLGYKEGIVT LMEFTWTHGC
VIESGEFRHG PLEIVEPGVP FLFLLGNDES RHTTERAINF VKQRTDNVIV IDYAEISQGL
HPWLAPFLMF VPMEWLCYYL SIYKDHNPDE RRYYGGLVEY
