ID   NANK_VIBC3              Reviewed;         287 AA.
AC   A5F7C0; C3M1H6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=VC0395_A1379, VC395_1896;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
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; CP000627; ABQ20894.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP09892.1; -; Genomic_DNA.
DR   RefSeq; WP_001259414.1; NZ_JAACZH010000016.1.
DR   AlphaFoldDB; A5F7C0; -.
DR   SMR; A5F7C0; -.
DR   STRING; 345073.VC395_1896; -.
DR   EnsemblBacteria; ABQ20894; ABQ20894; VC0395_A1379.
DR   GeneID; 57740425; -.
DR   KEGG; vco:VC0395_A1379; -.
DR   KEGG; vcr:VC395_1896; -.
DR   PATRIC; fig|345073.21.peg.1836; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_0_4_6; -.
DR   OMA; DANCAGM; -.
DR   UniPathway; UPA00629; UER00681.
DR   Proteomes; UP000000249; Chromosome 2.
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..287
FT                   /note="N-acetylmannosamine kinase"
FT                   /id="PRO_1000073168"
FT   BINDING         5..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         131..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01234"
SQ   SEQUENCE   287 AA;  30518 MW;  D3AB0B5C92D56A6F CRC64;
     MRTLAIDIGG TKIALAIVEE GTIIQRYQIA TPVVQDVTKF VQAILEKVTE WLPSIDYVGV
     STTGYVTPEG ITSINPETLN FPVPFPLAQT LEQLTNKPVS ILNDAQAAAW FEFVQLKNPS
     LNMAFITVST GVGGGIIIDG KLHKGNSGLA GHIGHMSVAI EGPLCGCGQR GCVESMASGN
     AIQKESEATF TETMSNVELF KQAAFNPKAE AIINRSVQAV ATLCCNLKAC LDLDIIVLGG
     GIGLAEGYLE RLNKAIQSRP SVFHIPVTPA HGDYDACLLG AAFQFKE