ID   NAGK_SHIF8              Reviewed;         303 AA.
AC   Q0T5R7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=N-acetyl-D-glucosamine kinase;
DE            EC=2.7.1.59;
DE   AltName: Full=GlcNAc kinase;
GN   Name=nagK; OrderedLocusNames=SFV_1139;
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-acetyl-D-glucosamine
CC       (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-
CC       D-glucosamine 6-phosphate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SIMILARITY: Belongs to the ROK (nagC/xylR) family. NagK subfamily.
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DR   EMBL; CP000266; ABF03348.1; -; Genomic_DNA.
DR   RefSeq; YP_688653.1; -.
DR   SMR; Q0T5R7; 1-303.
DR   GeneID; 4208953; -.
DR   GenomeReviews; CP000266_GR; SFV_1139.
DR   KEGG; sfv:SFV_1139; -.
DR   HOGENOM; Q0T5R7; -.
DR   OMA; Q0T5R7; HVERFME.
DR   BioCyc; SFLE373384:SFV_1139-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:HAMAP.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:HAMAP.
DR   HAMAP; MF_01271; -; 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    303       N-acetyl-D-glucosamine kinase.
FT                                /FTId=PRO_0000301942.
FT   NP_BIND       4     11       ATP (Potential).
FT   NP_BIND     133    140       ATP (Potential).
FT   METAL       157    157       Zinc (By similarity).
FT   METAL       177    177       Zinc (By similarity).
FT   METAL       179    179       Zinc (By similarity).
FT   METAL       184    184       Zinc (By similarity).
SQ   SEQUENCE   303 AA;  32987 MW;  65572B2CCFEBFBA5 CRC64;
     MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DQRFGCKGSV
     GIGIPGMPET EDGKLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT
     QYPLVMGLIL GTGVGGGLVF NGKPITGKSY ITGEFGHMRL PVDALTMMGL DFPLRRCGCG
     QHGCIENYLS GRGFAWLYQH YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVSLGNI
     LTIVDPDLVV IGGGLSNFPA ITTQLADRLP CHLLPVARVP RIERARHGDA GGMRGAAFLH
     LTD
//