ID   NANK_SALPK              Reviewed;         291 AA.
AC   B5BGP2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=SSPA2991;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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; FM200053; CAR61240.1; -; Genomic_DNA.
DR   RefSeq; WP_000208976.1; NC_011147.1.
DR   AlphaFoldDB; B5BGP2; -.
DR   SMR; B5BGP2; -.
DR   KEGG; sek:SSPA2991; -.
DR   HOGENOM; CLU_036604_0_4_6; -.
DR   OMA; APNIDWR; -.
DR   UniPathway; UPA00629; UER00681.
DR   Proteomes; UP000001869; 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_1000139694"
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;  30078 MW;  DB0B005C29194A63 CRC64;
     MTTLAIDIGG TKLAAALIDN NLRISQRREL PTPASKTPDA LREALKALVE PLRAEARQVA
     IASTGIIQEG MLLALNPHNL GGLLHFPLVQ TLEAIAGLPT LAVNDAQAAA WAEYHALPDD
     IRDMVFITVS TGVGGGVVCD GKLLTGKGGL AGHLGHTLAD PHGPVCGCGR VGCVEAIASG
     RGMAAAARDD LAGCDAKTLF IRAGEGHQQA RHLVSQSAQV IARMIADVKA TTDCQCVVIG
     GSVGLAEGYL EQVRAFLMQE PAPYHVALSA ARYRHDAGLL GAALLAQGDT L