KT3K_ECO57
ID KT3K_ECO57 Reviewed; 286 AA.
AC P58065;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable ketoamine kinase YniA;
DE EC=2.7.1.- {ECO:0000250|UniProtKB:Q9H479};
GN Name=yniA; OrderedLocusNames=Z2754, ECs2431;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Ketoamine kinase that phosphorylates ketoamines on the third
CC carbon of the sugar moiety to generate ketoamine 3-phosphate.
CC {ECO:0000250|UniProtKB:Q9H479}.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
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DR EMBL; AE005174; AAG56711.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35854.1; -; Genomic_DNA.
DR PIR; C85781; C85781.
DR PIR; G90932; G90932.
DR RefSeq; NP_310458.1; NC_002695.1.
DR RefSeq; WP_000267654.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; P58065; -.
DR SMR; P58065; -.
DR STRING; 155864.EDL933_2684; -.
DR PRIDE; P58065; -.
DR EnsemblBacteria; AAG56711; AAG56711; Z2754.
DR EnsemblBacteria; BAB35854; BAB35854; ECs_2431.
DR GeneID; 66674381; -.
DR GeneID; 913778; -.
DR KEGG; ece:Z2754; -.
DR KEGG; ecs:ECs_2431; -.
DR PATRIC; fig|386585.9.peg.2545; -.
DR eggNOG; COG3001; Bacteria.
DR HOGENOM; CLU_036517_0_0_6; -.
DR OMA; GSFYSAY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Probable ketoamine kinase YniA"
FT /id="PRO_0000216343"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 91..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ SEQUENCE 286 AA; 32475 MW; 2D7AAA4AE229F787 CRC64;
MWQAISRLLS EQLGEGEIEL RNELPGGEVH AAWHLRYAGH DFFVKCDERE LLPGFTAEAD
QLELLSRSKT VTVPKVWAVG ADRDYSFLVM DYLPPRPLDA HSAFILGQQI ARLHQWSDQP
QFGLDFDNSL STTPQPNTWQ RRWSTFFAEQ RIGWQLELAA EKGIAFGNID AIVEHIQQRL
ASHQPQPSLL HGDLWSGNCA LGPDGPYIFD PACYWGDREC DLAMLPLHTE QPPQIYDGYQ
SVSPLPADFL ERQPVYQLYT LLNRARLFGG QHLVIAQQSL DRLLAA