ID GLMU_SALTY STANDARD; PRT; 456 AA. AC Q8ZKX0; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 02-MAY-2006, entry version 21. 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 Co(2+) ion per subunit (By similarity). CC -!- PATHWAY: Peptidoglycan biosynthesis; lipopolysaccharide CC biosynthesis (lipid A biosynthesis); UDP-N-acetylglucosamine from CC fructose-6-P: step 3. CC -!- PATHWAY: Peptidoglycan biosynthesis; lipopolysaccharide CC biosynthesis (lipid A biosynthesis); UDP-N-acetylglucosamine from CC fructose-6-P: last step. 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 HSSP; P17114; 1HV9. DR SMR; Q8ZKX0; 3-451. DR GenomeReviews; AE006468_GR; STM3862. DR BioCyc; STYP99287:STM3862-MONOMER; -. DR HAMAP; MF_01631; -; 1. DR InterPro; IPR005882; GlmU. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR001228; ISPD_synthase. DR InterPro; IPR011004; Trimer_LpxA_like. DR Pfam; PF00132; Hexapep; 7. DR Pfam; PF01128; IspD; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. KW Acyltransferase; Cell shape; Cell wall; Cobalt; Complete proteome; KW Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Repeat; Transferase. FT CHAIN 1 456 Bifunctional protein glmU. FT /FTId=PRO_0000233838. FT ACT_SITE 105 105 UDP-N-acetylglucosamine pyrophosphorylase FT (By similarity). FT ACT_SITE 227 227 UDP-N-acetylglucosamine pyrophosphorylase FT (By similarity). FT METAL 105 105 Cobalt (By similarity). FT METAL 227 227 Cobalt (By similarity). FT BINDING 76 76 Substrate (By similarity). FT BINDING 82 82 Substrate (By similarity). FT BINDING 103 103 Substrate (By similarity). FT BINDING 154 154 Substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 405 405 Acetyl-CoA (By similarity). FT BINDING 423 423 Acetyl-CoA (By 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 //