ID   KT3K_VIBCH              Reviewed;         288 AA.
AC   Q9KRU5;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable ketoamine kinase VC_1539;
DE            EC=2.7.1.- {ECO:0000250|UniProtKB:Q9H479};
GN   OrderedLocusNames=VC_1539;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE003852; AAF94693.1; -; Genomic_DNA.
DR   PIR; G82186; G82186.
DR   RefSeq; NP_231179.1; NC_002505.1.
DR   RefSeq; WP_000267456.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KRU5; -.
DR   SMR; Q9KRU5; -.
DR   STRING; 243277.VC_1539; -.
DR   DNASU; 2613918; -.
DR   EnsemblBacteria; AAF94693; AAF94693; VC_1539.
DR   KEGG; vch:VC_1539; -.
DR   PATRIC; fig|243277.26.peg.1467; -.
DR   eggNOG; COG3001; Bacteria.
DR   HOGENOM; CLU_036517_0_0_6; -.
DR   OMA; GSFYSAY; -.
DR   BioCyc; VCHO:VC1539-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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..288
FT                   /note="Probable ketoamine kinase VC_1539"
FT                   /id="PRO_0000216348"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WI99"
FT   BINDING         92..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ   SEQUENCE   288 AA;  33770 MW;  1CE7932E20EA06A3 CRC64;
     MWPAIIQQLS EQLGKDFHLV EKEKVHGGDI NECFMVSDGI DRYFVKTNQR EYLTKFTAEV
     ENLRVMRESN TVQVPEYILH GTSKTHAYLV LNYLATKPLD DAERSYEFGV QLANLHRWGE
     QKEFGFDIDN YIGATVQPNP WHKKWALFFA EQRIGWQLQL MQEKGVNLTN INEFVEMVKT
     RLANHSPRPS LLHGDLWFGN VANIVNGPLC FDPACYWGDR ECDIALAEWF GGFQPEFFQG
     YESVWPLDWG YEERKDIYNL YHVLNHYNQF GGHYLDEAQK LIEKILSY