KT3K_THET8
ID KT3K_THET8 Reviewed; 262 AA.
AC Q5SJ35;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable ketoamine kinase TTHA1179 {ECO:0000305};
DE EC=2.7.1.- {ECO:0000269|PubMed:17681011};
GN OrderedLocusNames=TTHA1179;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 and ribuloselysine, on the third carbon of the sugar
CC moiety to generate ketoamine 3-phosphate (PubMed:17681011). Has higher
CC activity on free lysine (erythruloselysine and ribuloselysine), than on
CC ribuloselysine and erythruloselysine residues on glycated proteins
CC (PubMed:17681011). {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(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(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=58 uM for free ribuloselysine {ECO:0000269|PubMed:17681011};
CC KM=6 uM for free erythruloselysine {ECO:0000269|PubMed:17681011};
CC Vmax=450 nmol/min/mg enzyme with free ribuloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=770 nmol/min/mg enzyme with free erythruloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=7 nmol/min/mg enzyme with ribuloselysyl-protein (lysozyme) as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=4.2 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; AP008226; BAD71002.1; -; Genomic_DNA.
DR RefSeq; WP_011228495.1; NC_006461.1.
DR RefSeq; YP_144445.1; NC_006461.1.
DR AlphaFoldDB; Q5SJ35; -.
DR SMR; Q5SJ35; -.
DR STRING; 300852.55772561; -.
DR EnsemblBacteria; BAD71002; BAD71002; BAD71002.
DR GeneID; 3168142; -.
DR KEGG; ttj:TTHA1179; -.
DR PATRIC; fig|300852.9.peg.1159; -.
DR eggNOG; COG3001; Bacteria.
DR HOGENOM; CLU_036517_0_1_0; -.
DR OMA; GSFYSAY; -.
DR PhylomeDB; Q5SJ35; -.
DR Proteomes; UP000000532; 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..262
FT /note="Probable ketoamine kinase TTHA1179"
FT /id="PRO_0000448293"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 79..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ SEQUENCE 262 AA; 29325 MW; 0DBF94554835F396 CRC64;
MDPLALLRKA GLEAEGPALP LHGGDISRVW RVGRFVVKTA QDPPPGLFRA EARGLQALAE
RGVRVPRVHW VGEEGLVLAY LEPGPEDWEG LARTLAALHR RREGSYLAEP GFLGTFPLPG
REGGEWTAFF YERCVLPLLE ATWDRLQGLG PKVEALYQRP LPAEGPAPLH GDLWHGNVYF
AREGPALLDP SFFVGERGVD LAMMRLFGGF PRRFWEVYGE LYPVPEEVER ALPRYQVYYL
LAHVHFFGQG YLGALWRAIS AS
