ID   FRLB_ECO57              Reviewed;         340 AA.
AC   Q8X844;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Fructoselysine 6-phosphate deglycase {ECO:0000250|UniProtKB:P0AC00};
DE            EC=3.5.-.- {ECO:0000250|UniProtKB:P0AC00};
GN   Name=frlB; OrderedLocusNames=Z4732, ECs4222;
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 conversion of fructoselysine 6-
CC       phosphate to glucose 6-phosphate and lysine. Functions in a
CC       fructoselysine degradation pathway that allows E.coli to grow on
CC       fructoselysine or psicoselysine. {ECO:0000250|UniProtKB:P0AC00}.
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:0000250|UniProtKB:P0AC00};
CC   -!- PATHWAY: Carbohydrate metabolism; fructoselysine degradation; D-glucose
CC       6-phosphate and lysine from fructoselysine: step 2/2.
CC       {ECO:0000250|UniProtKB:P0AC00}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000250|UniProtKB:P0AC00}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG58479.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB37645.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG58479.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB37645.1; ALT_INIT; Genomic_DNA.
DR   PIR; C86002; C86002.
DR   PIR; F91156; F91156.
DR   RefSeq; NP_312249.2; NC_002695.1.
DR   RefSeq; WP_001301824.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X844; -.
DR   SMR; Q8X844; -.
DR   STRING; 155864.EDL933_4577; -.
DR   EnsemblBacteria; AAG58479; AAG58479; Z4732.
DR   EnsemblBacteria; BAB37645; BAB37645; ECs_4222.
DR   GeneID; 915923; -.
DR   KEGG; ece:Z4732; -.
DR   KEGG; ecs:ECs_4222; -.
DR   PATRIC; fig|386585.9.peg.4407; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_012520_3_0_6; -.
DR   OMA; LMEMQWI; -.
DR   UniPathway; UPA00784; UER00770.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Repeat.
FT   CHAIN           1..340
FT                   /note="Fructoselysine 6-phosphate deglycase"
FT                   /id="PRO_0000136594"
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;  38546 MW;  6F9A9168208A7B74 CRC64;
     MLDIDKSTVD FLVTENMVQE VEKVLSHDVP LVHTIVEEMV KRDIDRIYFV ACGSPLNAAQ
     TAKHLADRFS DLQVYAISGW EFCDNTPYRL DARCAVIGVS DYGKTEEVIK ALELGRACGA
     LTAAFTKRAD SPITSAAEFS IDYQADCIWE IHLLLCYSVV LEMITRLAPH AEIGKIKNDL
     KQLPNALGYL VRTWEEKGRQ LGELASQWPM IYTVAAGPLR PLGYKEGIVT LMEFTWTHGC
     VIESGEFRHG PLEIVEPGVP FLFLLGNDES RHTTERAINF VKQRTDNVIV IDYAAISQGL
     HPWLAPFLMF VPMEWLCYYL SIYKDHNPDE RRYYGGLVEY