ID NANK_SHIF8 Reviewed; 291 AA. AC Q0T068; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 18. DE RecName: Full=N-acetylmannosamine kinase; DE EC=2.7.1.60; DE AltName: Full=N-acetyl-D-mannosamine kinase; DE AltName: Full=ManNAc kinase; GN Name=nanK; OrderedLocusNames=SFV_3247; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16822325; DOI=10.1186/1471-2164-7-173; RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., RA Jin Q.; RT "Complete genome sequence of Shigella flexneri 5b and comparison with RT Shigella flexneri 2a."; RL BMC Genomics 7:173-173(2006). CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine CC (ManNAc) to ManNAc-6-P (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + N-acyl-D-mannosamine = ADP + N-acyl-D- CC mannosamine 6-phosphate. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminic acid CC degradation; D-fructose 6-phosphate from N-acetylneuraminic acid: CC step 2/5. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the ROK (nagC/xylR) family. NanK subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000266; ABF05297.1; -; Genomic_DNA. DR RefSeq; YP_690602.1; -. DR SMR; Q0T068; 1-289. DR GeneID; 4209285; -. DR GenomeReviews; CP000266_GR; SFV_3247. DR KEGG; sfv:SFV_3247; -. DR HOGENOM; Q0T068; -. DR OMA; Q0T068; EYQALEG. DR BioCyc; SFLE373384:SFV_3247-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:HAMAP. DR HAMAP; MF_01234; -; 1. DR InterPro; IPR000600; ROK. DR Pfam; PF00480; ROK; 1. DR PROSITE; PS01125; ROK; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Metal-binding; Nucleotide-binding; Transferase; Zinc. FT CHAIN 1 291 N-acetylmannosamine kinase. FT /FTId=PRO_0000301461. FT NP_BIND 5 12 ATP (Potential). FT NP_BIND 132 139 ATP (Potential). FT METAL 156 156 Zinc (By similarity). FT METAL 166 166 Zinc (By similarity). FT METAL 168 168 Zinc (By similarity). FT METAL 173 173 Zinc (By similarity). 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 //