ID B7NR32_ECO7I Unreviewed; 456 AA. AC B7NR32; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 14-APR-2009, entry version 3. DE SubName: Full=Fused N-acetyl glucosamine-1-phosphate uridyltransferase ; glucosamine-1-phosphate acetyl transferase; DE EC=2.7.7.23; GN Name=glmU; OrderedLocusNames=ECIAI39_4334; OS Escherichia coli O7:K1 (strain IAI39 / ExPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). 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: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. 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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; CU928164; CAR20440.1; -; Genomic_DNA. DR RefSeq; YP_002410209.1; -. DR GeneID; 7151521; -. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR018357; Hexapep_transf_CS. 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. SQ SEQUENCE 456 AA; 49222 MW; 68947CA5BE6D553B CRC64; MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ FEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK AGHLTYLGDA EVGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VGENALAISR VPQSQKEGWR RPVKKK //