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FRLD_SHIFL
ID   FRLD_SHIFL              Reviewed;         261 AA.
AC   Q83JB1;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Fructoselysine 6-kinase {ECO:0000250|UniProtKB:P45543};
DE            EC=2.7.1.218 {ECO:0000250|UniProtKB:P45543};
GN   Name=frlD; OrderedLocusNames=SF3392, S4370;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructoselysine
CC       to fructoselysine 6-phosphate. May function in a fructoselysine
CC       degradation pathway that allows S.flexneri to grow on fructoselysine or
CC       psicoselysine. {ECO:0000250|UniProtKB:P45543}.
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:0000250|UniProtKB:P45543};
CC   -!- PATHWAY: Carbohydrate metabolism; fructoselysine degradation; D-glucose
CC       6-phosphate and lysine from fructoselysine: step 1/2.
CC       {ECO:0000250|UniProtKB:P45543}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P45543}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN44854.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19324.1; -; Genomic_DNA.
DR   RefSeq; NP_709147.1; NC_004337.2.
DR   RefSeq; WP_000853346.1; NZ_WPGW01000003.1.
DR   AlphaFoldDB; Q83JB1; -.
DR   SMR; Q83JB1; -.
DR   STRING; 198214.SF3392; -.
DR   DNASU; 1080578; -.
DR   EnsemblBacteria; AAN44854; AAN44854; SF3392.
DR   EnsemblBacteria; AAP19324; AAP19324; S4370.
DR   GeneID; 1026966; -.
DR   GeneID; 58388145; -.
DR   KEGG; sfl:SF3392; -.
DR   KEGG; sfx:S4370; -.
DR   PATRIC; fig|198214.7.peg.4005; -.
DR   HOGENOM; CLU_027634_13_0_6; -.
DR   OMA; DYGFVSC; -.
DR   OrthoDB; 1604782at2; -.
DR   UniPathway; UPA00784; UER00769.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..261
FT                   /note="Fructoselysine 6-kinase"
FT                   /id="PRO_0000080067"
SQ   SEQUENCE   261 AA;  28320 MW;  24EEB8CED500C5C4 CRC64;
     MKTLATIGDN CVDIYPQLNK AFSGGNAVNV AVYCTRYGIQ PGCITWVGDD DYGTKLKQDL
     ARMGVDISHV HTKHGVTAQT QVELHDNDRV FGDYTEGVMA DFALSEEDYA WLAQYDIVHA
     AIWGHAEDAF PQLHAAGKLT AFDFSDKWDS PLWQTLVPHL DFAFASAPQE DEALRLKMKA
     IVARGAGTVI VTLGENGSIA WDGAQFWRQA PEPVTVIDTM GAGDSFIAGF LCGWSAGMTL
     PQAMAQGTAC AAKTIQYHGA W
 
 
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