NANK_ECO55
ID NANK_ECO55 Reviewed; 291 AA.
AC B7LHT0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, 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};
GN OrderedLocusNames=EC55989_3635;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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}.
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; CU928145; CAU99879.1; -; Genomic_DNA.
DR RefSeq; WP_000209017.1; NC_011748.1.
DR AlphaFoldDB; B7LHT0; -.
DR SMR; B7LHT0; -.
DR EnsemblBacteria; CAU99879; CAU99879; EC55989_3635.
DR KEGG; eck:EC55989_3635; -.
DR HOGENOM; CLU_036604_0_4_6; -.
DR OMA; APNIDWR; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000000746; 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_1000164989"
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; 29643 MW; 9CD0D90C9C1DFE51 CRC64;
MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS PLQAHAQRVA
IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT IAINDAQAAA WAEYQALEGD
ITDMVFITVS TGVGGGVVSG GKLLTGPGGL AGHIGHTLAD PHGPVCGCGR TGCVEAIASG
RGIAAAAQGE LAGADARTIF TRAGQGDEQA QQLIHLSART LARLIADIKA TTDCQCVVVG
GSVGLAEGYL ALVEMYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L