KT3K_STAA8
ID KT3K_STAA8 Reviewed; 288 AA.
AC Q2FV31;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Probable ketoamine kinase SAOUHSC_02908;
DE EC=2.7.1.- {ECO:0000269|PubMed:17681011};
GN OrderedLocusNames=SAOUHSC_02908 {ECO:0000312|EMBL:ABD31904.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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=13 uM for free erythruloselysine {ECO:0000269|PubMed:17681011};
CC KM=44 uM for ribuloselysyl-protein {ECO:0000269|PubMed:17681011};
CC KM=42 uM for erythruloselysyl-protein {ECO:0000269|PubMed:17681011};
CC Vmax=1300 nmol/min/mg enzyme with free ribuloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=1930 nmol/min/mg enzyme with free erythruloselysine as substrate
CC {ECO:0000269|PubMed:17681011};
CC Vmax=220 nmol/min/mg enzyme with ribuloselysyl-protein (lysozyme) as
CC substrate {ECO:0000269|PubMed:17681011};
CC Vmax=78 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; CP000253; ABD31904.1; -; Genomic_DNA.
DR RefSeq; WP_001005511.1; NZ_LS483365.1.
DR RefSeq; YP_501361.1; NC_007795.1.
DR AlphaFoldDB; Q2FV31; -.
DR SMR; Q2FV31; -.
DR STRING; 1280.SAXN108_2859; -.
DR EnsemblBacteria; ABD31904; ABD31904; SAOUHSC_02908.
DR GeneID; 3921360; -.
DR KEGG; sao:SAOUHSC_02908; -.
DR PATRIC; fig|93061.5.peg.2629; -.
DR eggNOG; COG3001; Bacteria.
DR HOGENOM; CLU_036517_0_1_9; -.
DR OMA; GSFYSAY; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
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..288
FT /note="Probable ketoamine kinase SAOUHSC_02908"
FT /id="PRO_0000448292"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 86..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ SEQUENCE 288 AA; 32988 MW; 5204A2431DED99D5 CRC64;
MNEQWLEHLP LKDIKEISPV SGGDVNEAYR VETDTDTFFL LVQRGRKESF YAAEIAGLNE
FERAGITAPR VIASGEVNGD AYLVMTYLEE GASGSQRQLG QLVAQLHSQQ QEEGKFGFSL
PYEGGDISFD NHWQDDWCTI FVDKRLDHLK DELLNRGLWD ANDIKVYDKV RRQIVAELEK
HQSKPSLLHG DLWGGNYMFL QDGRPALFDP APLYGDREFD IGITTVFGGF TSEFYDAYNK
HYPLAKGASY RLEFYRLYLL MVHLLKFGEM YRDSVAHSMD KILQDTTS
