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KT3K_ECOLI
ID   KT3K_ECOLI              Reviewed;         286 AA.
AC   P77739;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Probable ketoamine kinase YniA;
DE            EC=2.7.1.- {ECO:0000250|UniProtKB:Q9H479};
GN   Name=yniA; OrderedLocusNames=b1725, JW1714;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION.
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 on the third
CC       carbon of the sugar moiety to generate ketoamine 3-phosphate (By
CC       similarity). Its precise substrate are unknown: does not have
CC       ribulosamine and/or erythrulosamine 3-kinase activity in vitro
CC       (PubMed:17681011). {ECO:0000250|UniProtKB:Q9H479,
CC       ECO:0000269|PubMed:17681011}.
CC   -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74795.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15501.1; -; Genomic_DNA.
DR   PIR; E64931; E64931.
DR   RefSeq; NP_416239.1; NC_000913.3.
DR   RefSeq; WP_000267650.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P77739; -.
DR   SMR; P77739; -.
DR   BioGRID; 4263073; 24.
DR   DIP; DIP-12775N; -.
DR   IntAct; P77739; 6.
DR   STRING; 511145.b1725; -.
DR   jPOST; P77739; -.
DR   PaxDb; P77739; -.
DR   PRIDE; P77739; -.
DR   EnsemblBacteria; AAC74795; AAC74795; b1725.
DR   EnsemblBacteria; BAA15501; BAA15501; BAA15501.
DR   GeneID; 946236; -.
DR   KEGG; ecj:JW1714; -.
DR   KEGG; eco:b1725; -.
DR   PATRIC; fig|1411691.4.peg.531; -.
DR   EchoBASE; EB3742; -.
DR   eggNOG; COG3001; Bacteria.
DR   HOGENOM; CLU_036517_0_0_6; -.
DR   InParanoid; P77739; -.
DR   OMA; GSFYSAY; -.
DR   PhylomeDB; P77739; -.
DR   BioCyc; EcoCyc:G6930-MON; -.
DR   PRO; PR:P77739; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IBA:GO_Central.
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_0000216342"
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;  32459 MW;  40E4CA5305BD5138 CRC64;
     MWQAISRLLS EQLGEGEIEL RNELPGGEVH AAWHLRYAGH DFFVKCDERE LLPGFTAEAD
     QLELLSRSKT VTVPKVWAVG ADRDYSFLVM DYLPPRPLDA HSAFILGQQI ARLHQWSDQP
     QFGLDFDNAL STTPQPNTWQ RRWSTFFAEQ RIGWQLELAA EKGIAFGNID AIVEHIQQRL
     ASHQPQPSLL HGDLWSGNCA LGPDGPYIFD PACYWGDREC DLAMLPLHTE QPPQIYDGYQ
     SVSPLPADFL ERQPVYQLYT LLNRARLFGG QHLVIAQQSL DRLLAA
 
 
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