FRLD_ECOLI
ID FRLD_ECOLI Reviewed; 261 AA.
AC P45543; Q2M739;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Fructoselysine 6-kinase {ECO:0000303|PubMed:12147680};
DE EC=2.7.1.218 {ECO:0000269|PubMed:12147680};
GN Name=frlD {ECO:0000303|PubMed:12147680}; Synonyms=yhfQ;
GN OrderedLocusNames=b3374, JW3337;
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, PATHWAY,
RP 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, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND PATHWAY.
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 ATP-dependent phosphorylation of fructoselysine
CC to fructoselysine 6-phosphate (PubMed:12147680). Functions in a
CC fructoselysine degradation pathway that allows E.coli to grow on
CC fructoselysine or psicoselysine (PubMed:12147680, PubMed:14641112). To
CC a much lesser extenst, is also able to phosphorylate psicoselysine
CC (PubMed:14641112). {ECO:0000269|PubMed:12147680,
CC ECO:0000269|PubMed:14641112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-fructosyl)-L-lysine = ADP + H(+) + N(6)-(6-
CC phospho-D-fructosyl)-L-lysine; Xref=Rhea:RHEA:28378,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61392,
CC ChEBI:CHEBI:61393, ChEBI:CHEBI:456216; EC=2.7.1.218;
CC Evidence={ECO:0000269|PubMed:12147680};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for fructoselysine {ECO:0000269|PubMed:12147680};
CC KM=50 uM for ATP {ECO:0000269|PubMed:12147680};
CC KM=10 mM for psicoselysine {ECO:0000269|PubMed:14641112};
CC Vmax=30 umol/min/mg enzyme with fructoselysine as substrate
CC {ECO:0000269|PubMed:12147680};
CC Vmax=9 umol/min/mg enzyme with psicoselysine as substrate
CC {ECO:0000269|PubMed:14641112};
CC -!- PATHWAY: Carbohydrate metabolism; fructoselysine degradation; D-glucose
CC 6-phosphate and lysine from fructoselysine: step 1/2.
CC {ECO:0000305|PubMed:12147680, ECO:0000305|PubMed:14641112}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12147680}.
CC -!- INTERACTION:
CC P45543; P0AG07: rpe; NbExp=5; IntAct=EBI-562037, EBI-546020;
CC P45543; P05704: trg; NbExp=5; IntAct=EBI-562037, EBI-557436;
CC -!- INDUCTION: Induced by fructoselysine and psicoselysine. Makes part of
CC the frl operon with FrlA, FrlB, FrlC and FrlR.
CC {ECO:0000269|PubMed:12147680, ECO:0000269|PubMed:14641112}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; U18997; AAA58171.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76399.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77917.1; -; Genomic_DNA.
DR PIR; A65132; A65132.
DR RefSeq; NP_417833.1; NC_000913.3.
DR RefSeq; WP_000853353.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P45543; -.
DR SMR; P45543; -.
DR BioGRID; 4262482; 9.
DR BioGRID; 852195; 5.
DR DIP; DIP-12326N; -.
DR IntAct; P45543; 9.
DR STRING; 511145.b3374; -.
DR PaxDb; P45543; -.
DR PRIDE; P45543; -.
DR EnsemblBacteria; AAC76399; AAC76399; b3374.
DR EnsemblBacteria; BAE77917; BAE77917; BAE77917.
DR GeneID; 947886; -.
DR KEGG; ecj:JW3337; -.
DR KEGG; eco:b3374; -.
DR PATRIC; fig|511145.12.peg.3467; -.
DR EchoBASE; EB2748; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_13_0_6; -.
DR InParanoid; P45543; -.
DR OMA; DYGFVSC; -.
DR PhylomeDB; P45543; -.
DR BioCyc; EcoCyc:G7726-MON; -.
DR BioCyc; MetaCyc:G7726-MON; -.
DR BRENDA; 2.7.1.218; 2026.
DR SABIO-RK; P45543; -.
DR UniPathway; UPA00784; UER00769.
DR PRO; PR:P45543; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019200; F:carbohydrate kinase activity; IDA:EcoCyc.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..261
FT /note="Fructoselysine 6-kinase"
FT /id="PRO_0000080066"
SQ SEQUENCE 261 AA; 28332 MW; 30ACC15F901480C4 CRC64;
MKTLATIGDN CVDIYPQLNK AFSGGNAVNV AVYCTRYGIQ PGCITWVGDD DYGTKLKQDL
ARMGVDISHV HTKHGVTAQT QVELHDNDRV FGDYTEGVMA DFALSEEDYA WLAQYDIVHA
AIWGHAEDAF PQLHAAGKLT AFDFSDKWDS PLWQTLVPHL DFAFASAPQE DETLRLKMKA
IVARGAGTVI VTLGENGSIA WDGAQFWRQA PEPVTVIDTM GAGDSFIAGF LCGWSAGMTL
PQAIAQGTAC AAKTIQYHGA W