NANK2_ECOL6
ID NANK2_ECOL6 Reviewed; 291 AA.
AC Q8FDU8;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=N-acetylmannosamine kinase;
DE EC=2.7.1.60;
DE AltName: Full=ManNAc kinase;
DE AltName: Full=N-acetyl-D-mannosamine kinase;
GN Name=nanK2; OrderedLocusNames=c3638;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC to ManNAc-6-P. {ECO:0000250}.
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;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN82086.1; -; Genomic_DNA.
DR RefSeq; WP_000629094.1; NC_004431.1.
DR AlphaFoldDB; Q8FDU8; -.
DR SMR; Q8FDU8; -.
DR STRING; 199310.c3638; -.
DR EnsemblBacteria; AAN82086; AAN82086; c3638.
DR KEGG; ecc:c3638; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_4_6; -.
DR OMA; DANCAGM; -.
DR BioCyc; ECOL199310:C3638-MON; -.
DR UniPathway; UPA00629; UER00681.
DR Proteomes; UP000001410; 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_0000095698"
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 30744 MW; 260BAD700BE3B4E4 CRC64;
MITLAVDIGG TKISAALISD DGSFLLKKQI STPHERCPDE MTGALRLLVS EMKGTAERFA
VASTGIINNG VLTALNPDNL GGLKEYPLKN IMEDITGLNG SVINDAQAAA WAEYTVLPKE
ICDMVFITVS TGVGGGIVVN RKLLTGVSGL AGHVGHILSG VTDTECGCGR RGCVEAVSSG
RAIMGAAKNK LAGYSTKYIF ELARQGYKEA EFLTERSAST IAELIVSLKL LLDCQVVVVG
GSVGLADGYV QKVSKHLSIY SEICNVMLFP AYFRSDSGLI GATLWDRDCI T