ID   NANK_CITK8              Reviewed;         290 AA.
AC   A8AQB2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=CKO_04625;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV15675.1; -; Genomic_DNA.
DR   RefSeq; WP_012135354.1; NC_009792.1.
DR   AlphaFoldDB; A8AQB2; -.
DR   SMR; A8AQB2; -.
DR   STRING; 290338.CKO_04625; -.
DR   EnsemblBacteria; ABV15675; ABV15675; CKO_04625.
DR   GeneID; 45138159; -.
DR   KEGG; cko:CKO_04625; -.
DR   HOGENOM; CLU_036604_0_4_6; -.
DR   OMA; APNIDWR; -.
DR   OrthoDB; 1130699at2; -.
DR   UniPathway; UPA00629; UER00681.
DR   Proteomes; UP000008148; 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; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..290
FT                   /note="N-acetylmannosamine kinase"
FT                   /id="PRO_1000066907"
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   290 AA;  29798 MW;  525AFAF8D0486A18 CRC64;
     MSTLAIDIGG TKLAAARVDD DLRIRERREL PTPASKTPDA LREALKVLVE PLQTTAQRVA
     IASTGIIREG ALLAINPHNL GGLLHFPLVP TLEDLTGLPT LAVNDAQAAA WAEYHALASD
     VRDMVFITVS TGVGGGVVSD GRLLTGMSGL AGHLGHTLAD PQGPVCGCGR RGCVEAIASG
     RGIAAAAQGS LAGCDARTVF AHAAAGNEQA VRLVQHSAQV VARLIADVKA TTDCQQVVIG
     GSVGLAEGYL AQVRHFLAQE PAVYQVALSA AHYRHDAGLL GAALLAQGDK