ID GLMU_PSYWF Reviewed; 455 AA. AC A5WHT0; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 14-OCT-2008, entry version 14. DE RecName: Full=Bifunctional protein glmU; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase; DE EC=2.7.7.23; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase; DE EC=2.3.1.157; GN Name=glmU; OrderedLocusNames=PsycPRwf_2281; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 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: Bacterial outer membrane biogenesis; LPS 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; CP000713; ABQ95221.1; -; Genomic_DNA. DR RefSeq; YP_001281171.1; -. DR GeneID; 5205575; -. DR GenomeReviews; CP000713_GR; PsycPRwf_2281. DR KEGG; prw:PsycPRwf_2281; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. 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; 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 Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Repeat; Transferase. FT CHAIN 1 455 Bifunctional protein glmU. FT /FTId=PRO_1000073649. FT REGION 1 228 Pyrophosphorylase (By similarity). FT REGION 10 13 Substrate binding (By similarity). FT REGION 80 81 Substrate binding (By similarity). FT REGION 229 249 Linker (By similarity). FT REGION 250 455 N-acetyltransferase (By similarity). FT ACT_SITE 362 362 Proton acceptor (By similarity). FT METAL 104 104 Magnesium (By similarity). FT METAL 226 226 Magnesium (By similarity). FT BINDING 75 75 Substrate (By similarity). FT BINDING 138 138 Substrate; via amide nitrogen (By FT similarity). FT BINDING 153 153 Substrate (By similarity). FT BINDING 168 168 Substrate (By similarity). FT BINDING 386 386 Acetyl-CoA (By similarity). FT BINDING 422 422 Acetyl-CoA; via amide nitrogen (By FT similarity). FT BINDING 439 439 Acetyl-CoA (By similarity). 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 //