ID GLMU_SALTY Reviewed; 456 AA. AC Q8ZKX0; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 29-APR-2008, entry version 35. DE Bifunctional protein glmU [Includes: UDP-N-acetylglucosamine DE pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate DE uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase DE (EC 2.3.1.157)]. GN Name=glmU; OrderedLocusNames=STM3862; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; 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 last two sequential reactions in the de CC novo biosynthetic pathway for UDP-GlcNAc. Responsible for the CC acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl CC transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc (By CC similarity). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-D-glucosamine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine CC biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D- CC glucosamine 6-phosphate (route II): step 2/2. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine CC biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D- CC glucosamine 1-phosphate: step 1/1. CC -!- PATHWAY: Context: Lipopolysaccharide (LPS) biosynthesis; lipid A CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE008880; AAL22720.1; -; Genomic_DNA. DR RefSeq; NP_462761.1; -. DR HSSP; P17114; 1HV9. DR SMR; Q8ZKX0; 3-451. DR GeneID; 1255389; -. DR GenomeReviews; AE006468_GR; STM3862. DR KEGG; stm:STM3862; -. DR NMPDR; fig|99287.1.peg.3735; -. DR BioCyc; STYP99287:STM3862-MON; -. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase...; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase act...; IEA:HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01631; -; 1. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR001228; ISPD_synthase. DR InterPro; IPR005882; UDP_GlcNAc_PyrPase. DR Pfam; PF00132; Hexapep; 7. DR Pfam; PF01128; IspD; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Repeat; Transferase. FT CHAIN 1 456 Bifunctional protein glmU. FT /FTId=PRO_0000233838. FT REGION 1 229 Pyrophosphorylase (By similarity). FT REGION 11 14 Substrate binding (By similarity). FT REGION 81 82 Substrate binding (By similarity). FT REGION 230 250 Linker (By similarity). FT REGION 251 456 N-acetyltransferase (By similarity). FT ACT_SITE 363 363 Proton acceptor (By similarity). FT METAL 105 105 Magnesium (By similarity). FT METAL 227 227 Magnesium (By similarity). FT BINDING 76 76 Substrate (By similarity). FT BINDING 140 140 Substrate; via amide nitrogen (By FT similarity). FT BINDING 154 154 Substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 387 387 Acetyl-CoA (By similarity). FT BINDING 405 405 Acetyl-CoA (By similarity). FT BINDING 423 423 Acetyl-CoA; via amide nitrogen (By FT similarity). FT BINDING 440 440 Acetyl-CoA (By similarity). SQ SEQUENCE 456 AA; 49198 MW; D0730ECD43D3E8DB CRC64; MLNSAMSVVI LAAGKGTRMY SDIPKVLHTL AGKPMVQHVI DAATKLGAAQ VHLVYGHGGE LLKQTLKDDK LNWVLQAEQL GTGHAMQQAA PFFSDDEDIL MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPSGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM KRWLSKLTNN NAQGEYYITD IIALAYQEGR EIAAVHPARI SETDGVNNRL QLSRLERIYQ AEQAEKLLLS GVMLRDPARF DLRGTLHCGM DVEIDANVII EGYVTLGHRV KIGAGCIIKN SVIGDDCEIS PYSVVEDAHL EAACTIGPFA RLRPGAELLA GAHVGNFVEM KKARLGKGSK AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTVIGDD VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VADNELVLSR VPQVHKQGWQ RPVKKK //