ID   NANK_ECO27              Reviewed;         291 AA.
AC   B7UJV5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=N-acetylmannosamine kinase {ECO:0000255|HAMAP-Rule:MF_01234};
DE            EC=2.7.1.60 {ECO:0000255|HAMAP-Rule:MF_01234};
DE   AltName: Full=ManNAc kinase {ECO:0000255|HAMAP-Rule:MF_01234};
DE   AltName: Full=N-acetyl-D-mannosamine kinase {ECO:0000255|HAMAP-Rule:MF_01234};
GN   Name=nanK {ECO:0000255|HAMAP-Rule:MF_01234}; OrderedLocusNames=E2348C_3494;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC       to ManNAc-6-P. {ECO:0000255|HAMAP-Rule:MF_01234}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine
CC         6-phosphate + H(+); Xref=Rhea:RHEA:23832, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16062, ChEBI:CHEBI:30616, ChEBI:CHEBI:57666,
CC         ChEBI:CHEBI:456216; EC=2.7.1.60; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01234};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 2/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01234}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01234}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01234}.
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DR   EMBL; FM180568; CAS11042.1; -; Genomic_DNA.
DR   RefSeq; WP_000209053.1; NC_011601.1.
DR   AlphaFoldDB; B7UJV5; -.
DR   SMR; B7UJV5; -.
DR   EnsemblBacteria; CAS11042; CAS11042; E2348C_3494.
DR   KEGG; ecg:E2348C_3494; -.
DR   HOGENOM; CLU_036604_0_4_6; -.
DR   OMA; APNIDWR; -.
DR   UniPathway; UPA00629; UER00681.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01234; ManNAc_kinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR023945; ManNAc_kinase_bac.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN           1..291
FT                   /note="N-acetylmannosamine kinase"
FT                   /id="PRO_1000164988"
FT   BINDING         5..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         132..139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
SQ   SEQUENCE   291 AA;  29695 MW;  CBBF7E6E00B0D2EB CRC64;
     MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPQA LRDALSALVS PLQAHAQRVA
     IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT IAINDAQAAA WAEYQALDGD
     ITDIVFITVS TGVGGGVVSG GKLRTGPGGL AGHIGHTLAD PHGPVCGCGR TGCVEAIASG
     RGIAAAAQGE LAGANAKTIF TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG
     GSVGLAEGYL ALVETYLAQE PEAFHVDLLA AHYRHDAGLL GAALLAQGEK L