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Database: UniProt
Entry: FRLD_ECOLI
LinkDB: FRLD_ECOLI
Original site: 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   24-JAN-2024, entry version 147.
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; Pseudomonadota; 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; 511145-b3374; -.
DR   EnsemblBacteria; AAC76399; AAC76399; b3374.
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   OrthoDB; 9792663at2; -.
DR   PhylomeDB; P45543; -.
DR   BioCyc; EcoCyc:G7726-MONOMER; -.
DR   BioCyc; MetaCyc:G7726-MONOMER; -.
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   CDD; cd01940; Fructoselysine_kinase_like; 1.
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   PANTHER; PTHR43320:SF3; PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43320; SUGAR KINASE; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 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
//
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