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NANK_SHIFL
ID   NANK_SHIFL              Reviewed;         291 AA.
AC   P59437;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=SF3258, S3475;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAN44722.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP18535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN44722.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18535.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_709015.4; NC_004337.2.
DR   RefSeq; WP_000153624.1; NZ_WPGW01000176.1.
DR   AlphaFoldDB; P59437; -.
DR   SMR; P59437; -.
DR   STRING; 198214.SF3258; -.
DR   EnsemblBacteria; AAN44722; AAN44722; SF3258.
DR   EnsemblBacteria; AAP18535; AAP18535; S3475.
DR   GeneID; 1026854; -.
DR   GeneID; 58391748; -.
DR   KEGG; sfl:SF3258; -.
DR   KEGG; sfx:S3475; -.
DR   PATRIC; fig|198214.7.peg.3861; -.
DR   HOGENOM; CLU_036604_0_4_6; -.
DR   OrthoDB; 1130699at2; -.
DR   UniPathway; UPA00629; UER00681.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..291
FT                   /note="N-acetylmannosamine kinase"
FT                   /id="PRO_0000095703"
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;  29698 MW;  1F180C9C589FC1E7 CRC64;
     MTILAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS PLQAHAQRVA
     IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT IAINDAQAAA WAEYQALEGD
     ITDMVFITVS TGVGGGVVSG GKLLTGPGGL AGHIGHTLAD PHGPVCGCGR TGCVEAIASG
     RGIAAAAQGE LAGADARTIF TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG
     GSVGLAEGYL ALVEMYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L
 
 
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