ID   NANK_SALTY              Reviewed;         291 AA.
AC   Q8ZLQ8;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JUN-2009, entry version 36.
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=STM3336;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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.
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DR   EMBL; AE008853; AAL22205.1; -; Genomic_DNA.
DR   RefSeq; NP_462246.1; -.
DR   SMR; Q8ZLQ8; 1-289.
DR   GeneID; 1254859; -.
DR   GenomeReviews; AE006468_GR; STM3336.
DR   KEGG; stm:STM3336; -.
DR   HOGENOM; Q8ZLQ8; -.
DR   OMA; Q8ZLQ8; EYQALEG.
DR   BioCyc; MetaCyc:MON-13105; -.
DR   BioCyc; STYP99287:STM3336-MON; -.
DR   BRENDA; 2.7.1.60; 2.
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_0000095702.
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;  30078 MW;  DB0B005C29194A63 CRC64;
     MTTLAIDIGG TKLAAALIDN NLRISQRREL PTPASKTPDA LREALKALVE PLRAEARQVA
     IASTGIIQEG MLLALNPHNL GGLLHFPLVQ TLEAIAGLPT LAVNDAQAAA WAEYHALPDD
     IRDMVFITVS TGVGGGVVCD GKLLTGKGGL AGHLGHTLAD PHGPVCGCGR VGCVEAIASG
     RGMAAAARDD LAGCDAKTLF IRAGEGHQQA RHLVSQSAQV IARMIADVKA TTDCQCVVIG
     GSVGLAEGYL EQVRAFLMQE PAPYHVALSA ARYRHDAGLL GAALLAQGDT L
//