ID NANK_HAEI8 Reviewed; 300 AA. AC Q4QP43; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 20. 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=NTHI0230; OS Haemophilus influenzae (strain 86-028NP). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=281310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005; RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., RA Munson R.S. Jr.; RT "Genomic sequence of an otitis media isolate of nontypeable RT Haemophilus influenzae: comparative study with H. influenzae serotype RT d, strain KW20."; RL J. Bacteriol. 187:4627-4636(2005). 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; CP000057; AAX87204.1; -; Genomic_DNA. DR RefSeq; YP_247864.1; -. DR GeneID; 3429570; -. DR GenomeReviews; CP000057_GR; NTHI0230. DR KEGG; hit:NTHI0230; -. DR HOGENOM; Q4QP43; -. DR OMA; Q4QP43; KNDEKAT. DR BioCyc; HINF281310:NTHI0230-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 1 300 N-acetylmannosamine kinase. FT /FTId=PRO_0000301459. 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 300 AA; 31964 MW; ECDD3F41A7A8DED2 CRC64; MRCLALDIGG TKIAAAIVKN GEIEQRQQIH TPRENVVEGM HQALGKLLAD YEGQFDYVAV ASTGIINNGI LSALNPKNLG GLAEFPLKAS IAKHTDKPIG LLNDAQAATY AEYQLQNFEQ VSNFVFITVS TGVGGGIVLN QILQTGSRGI AGHIGHTLAD PNGAICGCGR RGCVEAIASG RAIEAVSSQW EDPCDPKEVF ERFRKNDEKA TALVERSAKA IANLIADLVI SLDIQKIAIG GSVGLAEGYL SLVEKYLQDF PSIYCCEIET AKFGQDAGLI GAAYWVKDVL LDKPEGTIYG //