ID Q8ZKX0 PRELIMINARY; PRT; 456 AA. AC Q8ZKX0; DT 01-MAR-2002 (TrEMBLrel. 20, Created) DT 01-MAR-2002 (TrEMBLrel. 20, Last sequence update) DT 01-OCT-2003 (TrEMBLrel. 25, Last annotation update) DE N-acetyl glucosamine-1-phosphate uridyltransferase (EC 2.7.7.23). 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. RC STRAIN=LT2; 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: Bifunctional enzyme responsible for the acetylation of CC Glc-N-1-P to give GlcNAc-1-P and the synthesis of 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 -!- PATHWAY: Peptidoglycan and lipopolysaccharide biosynthesis. 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; -. DR HSSP; P17114; 1HV9. DR GO; GO:0016740; F:transferase activity; IEA. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase act...; IEA. DR GO; GO:0009058; P:biosynthesis; IEA. DR GO; GO:0009103; P:lipopolysaccharide biosynthesis; IEA. DR InterPro; IPR005882; GlmU. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR005835; NTP_transferase. DR Pfam; PF00132; Hexapep; 7. DR Pfam; PF00483; NTP_transferase; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. KW Acyltransferase; Cell shape; Cell wall; Complete proteome; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Repeat; Transferase. 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 //