KT3K_LACPL
ID KT3K_LACPL Reviewed; 280 AA.
AC F9UPU7;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Probable ketoamine kinase lp_1983 {ECO:0000305};
DE EC=2.7.1.- {ECO:0000269|PubMed:17681011};
GN OrderedLocusNames=lp_1983;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17681011; DOI=10.1111/j.1742-4658.2007.05948.x;
RA Gemayel R., Fortpied J., Rzem R., Vertommen D., Veiga-da-Cunha M.,
RA Van Schaftingen E.;
RT "Many fructosamine 3-kinase homologues in bacteria are
RT ribulosamine/erythrulosamine 3-kinases potentially involved in protein
RT deglycation.";
RL FEBS J. 274:4360-4374(2007).
CC -!- FUNCTION: Ketoamine kinase that phosphorylates ketoamines, such as
CC erythruloselysine, erythrulosecadaverine, ribuloselysine and
CC ribulosecadaverine, on the third carbon of the sugar moiety to generate
CC ketoamine 3-phosphate (PubMed:17681011). Has higher activity on free
CC lysine (erythruloselysine and ribuloselysine), than on ribuloselysine
CC and erythruloselysine residues on glycated proteins (PubMed:17681011).
CC {ECO:0000269|PubMed:17681011}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-ribulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-
CC phospho-D-ribulosyl)-L-lysine; Xref=Rhea:RHEA:61400,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144590,
CC ChEBI:CHEBI:144611, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17681011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61401;
CC Evidence={ECO:0000269|PubMed:17681011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-(D-ribulosyl)-cadaverine = ADP + H(+) + N-(3-O-
CC phospho-D-ribulosyl)-cadaverine; Xref=Rhea:RHEA:61404,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144612,
CC ChEBI:CHEBI:144614, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17681011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61405;
CC Evidence={ECO:0000269|PubMed:17681011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-erythrulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-
CC phospho-D-erythrulosyl)-L-lysine; Xref=Rhea:RHEA:61408,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144617,
CC ChEBI:CHEBI:144618, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17681011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61409;
CC Evidence={ECO:0000269|PubMed:17681011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-(D-erythrulosyl)-cadaverine = ADP + H(+) + N-(3-O-
CC phospho-D-erythrulosyl)-cadaverine; Xref=Rhea:RHEA:61412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144619,
CC ChEBI:CHEBI:144620, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17681011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61413;
CC Evidence={ECO:0000269|PubMed:17681011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000269|PubMed:17681011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-erythrulosyl)-L-lysyl-[protein] = ADP + H(+) +
CC N(6)-(3-O-phospho-D-erythrulosyl)-L-lysyl-[protein];
CC Xref=Rhea:RHEA:61396, Rhea:RHEA-COMP:15794, Rhea:RHEA-COMP:15799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144587,
CC ChEBI:CHEBI:144624, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17681011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61397;
CC Evidence={ECO:0000269|PubMed:17681011};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for free ribuloselysine {ECO:0000269|PubMed:17681011};
CC KM=340 uM for free ribulosecadaverine {ECO:0000269|PubMed:17681011};
CC KM=60 uM for free erythruloselysine {ECO:0000269|PubMed:17681011};
CC KM=63 uM for free erythrulosecadaverine
CC {ECO:0000269|PubMed:17681011};
CC Vmax=510 nmol/min/mg enzyme with free ribuloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=2860 nmol/min/mg enzyme with free ribulosecadaverine as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=610 nmol/min/mg enzyme with free erythruloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=800 nmol/min/mg enzyme with free erythrulosecadaverine as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=16 nmol/min/mg enzyme with ribuloselysyl-protein (lysozyme) as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=3.8 nmol/min/mg enzyme with erythruloselysyl-protein (lysozyme)
CC as substrate {ECO:0000269|PubMed:17681011};
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
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DR EMBL; AL935263; CCC79236.1; -; Genomic_DNA.
DR RefSeq; WP_003644479.1; NC_004567.2.
DR RefSeq; YP_004889750.1; NC_004567.2.
DR AlphaFoldDB; F9UPU7; -.
DR SMR; F9UPU7; -.
DR DNASU; 1064115; -.
DR EnsemblBacteria; CCC79236; CCC79236; lp_1983.
DR GeneID; 57025561; -.
DR KEGG; lpl:lp_1983; -.
DR PATRIC; fig|220668.9.peg.1676; -.
DR eggNOG; COG3001; Bacteria.
DR HOGENOM; CLU_036517_0_1_9; -.
DR OMA; GSFYSAY; -.
DR PhylomeDB; F9UPU7; -.
DR BioCyc; LPLA220668:G1GW0-1700-MON; -.
DR Proteomes; UP000000432; 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; IDA:UniProtKB.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12149; PTHR12149; 1.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..280
FT /note="Probable ketoamine kinase lp_1983"
FT /id="PRO_0000448291"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 87..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ SEQUENCE 280 AA; 31841 MW; 9E5FEF8E7AAE1B6F CRC64;
MHLTKTWLAQ LPLTDIQQVQ PVSGGDINAA FQIITRHHQY FLKVQPHNDV TFFDHEVAGL
RLLGAVTKTP RVIASGTIAT DGYLLLDWLA TGTGSQSALG AAVAKVHHQH HAQFGLDHDF
TAGKLPKINH WQTDWATFYT QQRLDVLVNL AKEHHLWSET REMHYHRLRQ QLLQDSHMHT
VKPSLLHGDL WSGNYLFDTT GTPVLIDPDV FYGDREMDLA MTTIFGGFDT DFYQAYQAAY
PVAPGMQDRL PSYQLYYLLA HLNLFGETYG PAVDRILMQY
