ID A5WHT0_9GAMM Unreviewed; 455 AA. AC A5WHT0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 15-JAN-2008, entry version 7. DE Glucosamine-1-phosphate N-acetyltransferase / UDP-N-acetylglucosamine DE pyrophosphorylase (EC 2.3.1.157) (EC 2.7.7.23). GN ORFNames=PsycPRwf_2281; OS Psychrobacter sp. PRwf-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRwf-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. 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: Context: Lipopolysaccharide (LPS) biosynthesis; 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; CP000713; ABQ95221.1; -; Genomic_DNA. DR RefSeq; YP_001281171.1; -. DR GeneID; 5205575; -. DR InterPro; IPR005882; GlmU. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR001228; ISPD_synthase. DR Pfam; PF00132; Hexapep; 8. 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 Cytoplasm; Magnesium; Metal-binding; Multifunctional enzyme; KW Nucleotidyltransferase; Peptidoglycan synthesis; Repeat; Transferase. SQ SEQUENCE 455 AA; 49296 MW; 6074BD4D1C91F6F6 CRC64; MNNTLTTIIL AAGKGTRMQS AKPKVLQILA DKPLLAHVLD TCQSISVDKT IVVYGFGGDQ VQQAMTDYSL TWVEQTEQLG TGHAVKVALD ELPSTGKSLI LYGDVPLVSA ETLSRLKQAN VQGMSMLTLT VDNPFGLGRI KRDEQGNITA IVEQKDASEQ EQAIREINSG IYCVDNALLH QYLPNLSNDN AQQEYYLTDI VKMAVADGIA IAAIEPDYEF EIEGVNNRQQ LAQLERKWQA KLVEDLQVQG VQFADPNRVD IRGEVSVGQD VFVDINVVFK GKVSLGNNVT IEAGCMIKDS QIGDNVHIKP YCVFDDAQVA QGATIGPFAH LRPQTVLEKN TRLGNFVEIK KSRIGEGSKV NHLSYVGDAQ IGAGVNFGAG AITCNYDGVN KHQTIVGDNA FIGTNTSLVA PVTIGQTATI GAGSVITKNV EDNALAIGRG RQVQKDNYQR PEKKK //