ID   NAGK_SHISS              Reviewed;         303 AA.
AC   Q3Z2Z8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=N-acetyl-D-glucosamine kinase;
DE            EC=2.7.1.59;
DE   AltName: Full=GlcNAc kinase;
GN   Name=nagK; OrderedLocusNames=SSON_1139;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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.
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; CP000038; AAZ87864.1; -; Genomic_DNA.
DR   RefSeq; YP_310099.1; -.
DR   SMR; Q3Z2Z8; 1-303.
DR   GeneID; 3670303; -.
DR   GenomeReviews; CP000038_GR; SSON_1139.
DR   KEGG; ssn:SSON_1139; -.
DR   HOGENOM; Q3Z2Z8; -.
DR   OMA; Q3Z2Z8; HVERFME.
DR   BioCyc; SSON300269:SSO_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_0000270118.
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;  33032 MW;  02F935E34B3C90DC CRC64;
     MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DQRFGCKGSV
     GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT
     QYPLVMGLIL GTGVGGGLIF NGKPITGKSY ITGEFGHMRL PVDALTMMGL DFPLRRCGCG
     QIGCIENYLS GRGFAWLWQH YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI
     LTIVDSDLVV IGGGLSNFPA ITTQLADRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH
     LTD
//