ID NAGK_HAES1 Reviewed; 305 AA. AC Q0I4A5; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 05-MAY-2009, entry version 21. DE RecName: Full=N-acetyl-D-glucosamine kinase; DE EC=2.7.1.59; DE AltName: Full=GlcNAc kinase; GN Name=nagK; OrderedLocusNames=HS_1041; OS Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=205914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17172329; DOI=10.1128/JB.01422-06; RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., RA Xie G., Inzana T.J.; RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) RT strain 129Pt and comparison to Haemophilus ducreyi 35000HP and RT Haemophilus influenzae Rd."; RL J. Bacteriol. 189:1890-1898(2007). 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; CP000436; ABI25316.1; -; Genomic_DNA. DR RefSeq; YP_719253.1; -. DR GeneID; 4240539; -. DR GenomeReviews; CP000436_GR; HS_1041. DR KEGG; hso:HS_1041; -. DR NMPDR; fig|205914.1.peg.608; -. DR HOGENOM; Q0I4A5; -. DR OMA; Q0I4A5; TALDPHV. DR BioCyc; HSOM205914:HS_1041-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 1 305 N-acetyl-D-glucosamine kinase. FT /FTId=PRO_0000270107. FT NP_BIND 4 11 ATP (Potential). FT NP_BIND 133 140 ATP (Potential). FT METAL 157 157 Zinc (By similarity). FT METAL 178 178 Zinc (By similarity). FT METAL 180 180 Zinc (By similarity). FT METAL 185 185 Zinc (By similarity). SQ SEQUENCE 305 AA; 33529 MW; 8A9D05A5D20AFC32 CRC64; MYYGFDIGGT KIELAVFNEK LEKRYSERVD TPKHSYDEWL NVITHLVQKA DEKFACKGTV GIGVPGFVNQ ETGIAEITNI RVADNKPILK DLSERLGREV RAENDANCFA LSEAWDKDNQ QYPVVLGLIL GTGFGGGLVF NGKVHSGQSG MAGELGHLQL NYHALKLLGW DKAPIYECGC GNKACLDTYL SGRGFEMLYR DLQGKALSAK EIIRCFYDKD ESAVKFVELF IELCAISIGN IITALDPHVI ILGGGLSNFD YLYEALPKAL PQHLMRTAKV PLIKKAKFGD SGGVRGAAAL FLSRD //