KT3K_ENTFD
ID KT3K_ENTFD Reviewed; 277 AA.
AC Q3XZZ9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Probable ketoamine kinase HMPREF0351_12196 {ECO:0000305};
DE EC=2.7.1.- {ECO:0000269|PubMed:17681011};
GN ORFNames=HMPREF0351_12196 {ECO:0000312|EMBL:AFK59820.1};
OS Enterococcus faecium (strain ATCC BAA-472 / TX0016 / DO).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=333849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-472 / TX0016 / DO;
RX PubMed=22769602; DOI=10.1186/1471-2180-12-135;
RA Qin X., Galloway-Pena J.R., Sillanpaa J., Hyeob Roh J., Nallapareddy S.R.,
RA Chowdhury S., Bourgogne A., Choudhury T., Munzy D.M., Buhay C.J., Ding Y.,
RA Dugan-Rocha S., Liu W., Kovar C., Sodergren E., Highlander S.,
RA Petrosino J.F., Worley K.C., Gibbs R.A., Weinstock G.M., Murray B.E.;
RT "Complete genome sequence of Enterococcus faecium strain TX16 and
RT comparative genomic analysis of Enterococcus faecium genomes.";
RL BMC Microbiol. 12:135-135(2012).
RN [2]
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=185 uM for free ribuloselysine {ECO:0000269|PubMed:17681011};
CC KM=44 uM for free ribulosecadaverine {ECO:0000269|PubMed:17681011};
CC KM=15 uM for free erythruloselysine {ECO:0000269|PubMed:17681011};
CC KM=34 uM for free erythrulosecadaverine
CC {ECO:0000269|PubMed:17681011};
CC Vmax=730 nmol/min/mg enzyme with free ribuloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=1340 nmol/min/mg enzyme with free ribulosecadaverine as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=480 nmol/min/mg enzyme with free erythruloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=460 nmol/min/mg enzyme with free erythrulosecadaverine as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=40 nmol/min/mg enzyme with ribuloselysyl-protein (lysozyme) as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=80 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; CP003583; AFK59820.1; -; Genomic_DNA.
DR RefSeq; WP_002287963.1; NZ_AAAK03000025.1.
DR RefSeq; YP_006376802.1; NC_017960.1.
DR AlphaFoldDB; Q3XZZ9; -.
DR SMR; Q3XZZ9; -.
DR EnsemblBacteria; AFK59820; AFK59820; HMPREF0351_12196.
DR GeneID; 66455001; -.
DR KEGG; efu:HMPREF0351_12196; -.
DR HOGENOM; CLU_036517_0_1_9; -.
DR OMA; GSFYSAY; -.
DR Proteomes; UP000005269; 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..277
FT /note="Probable ketoamine kinase HMPREF0351_12196"
FT /id="PRO_0000448385"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 84..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ SEQUENCE 277 AA; 32236 MW; D44E145C8BAAAEA8 CRC64;
MDIQTVLSDL KLNGKVIPVV GGDVNQTYRI KTEHRAYFLK IHPNVKKGFF EAEVDGLKEL
SAFVRVPDTY MLGETSEGAY LLMEWIEPGK GDQRDLAAAL ANLHQQTAPQ FGFRKDNYLG
TLVQKNSFEE DWWTFFFKDR LESQISLAEE TNRWNVQRQE KYLRFKERVL KSVEPKKITP
RLLHGDLWSG NVFFDQQGHP VFVDPAVSYG NREQDIAMSQ LFGGFRPEFL DAYQTIFPLE
KGWKDRLPIY QLYYLLAHLN MFGESYGSQV DQLLENF
