ID C8KFW0_LISMO Unreviewed; 457 AA. AC C8KFW0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-DEC-2011, entry version 10. DE RecName: Full=Bifunctional protein GlmU; GN Name=glmU; ORFNames=LMMG_02757; OS Listeria monocytogenes F6900. OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393128; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F6900; RG The Broad Institute Genome Sequencing Platform; RA Borowsky M., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Wiedmann M., RA Swaminathan B., Lauer P., Portnoy D., Cossart P., Buchrieser C., RA Higgins D., Lander E., Galagan J., Nusbaum C., Birren B.; RT "The genome sequence of Listeria monocytogenes strain F6900."; RL Submitted (SEP-2009) 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: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate CC from alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase 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; AARU02000009; EEW23514.1; -; Genomic_DNA. DR ProteinModelPortal; C8KFW0; -. DR SMR; C8KFW0; 3-453. DR PATRIC; 27483816; VBILisMon69349_2864. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:HAMAP. DR GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_01631; GlmU; 1; -. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR005835; NTP_transferase. DR InterPro; IPR011004; Trimer_LpxA-like. DR PANTHER; PTHR22572:SF17; PTHR22572:SF17; 1. DR Pfam; PF00132; Hexapep; 4. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; Trimer_LpxA_like; 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. FT REGION 1 230 Pyrophosphorylase (By similarity). FT REGION 9 12 Substrate binding (By similarity). FT REGION 78 79 Substrate binding (By similarity). FT REGION 231 251 Linker (By similarity). FT REGION 252 457 N-acetyltransferase (By similarity). FT ACT_SITE 363 363 Proton acceptor (By similarity). FT METAL 103 103 Magnesium (By similarity). FT METAL 228 228 Magnesium (By similarity). FT BINDING 73 73 Substrate (By similarity). FT BINDING 140 140 Substrate; via amide nitrogen (By FT similarity). FT BINDING 155 155 Substrate (By similarity). FT BINDING 170 170 Substrate (By similarity). FT BINDING 387 387 Acetyl-CoA (By similarity). FT BINDING 423 423 Acetyl-CoA; via amide nitrogen (By FT similarity). FT BINDING 440 440 Acetyl-CoA (By similarity). SQ SEQUENCE 457 AA; 49781 MW; 24175DBC7601CE54 CRC64; MSKRYAVVLA AGQGTRMKSK LYKVLHPVCG KPMVEHVVDQ ISTLNVDKVV TIVGHGAEKV QEHLAGKSEF VKQDEQLGTA HAVLQAKAEL AGKDGVTLVV CGDTPLIEAS TMEALLKYHH EKRAKATILT TVIEDPTGYG RIIRDDLGIV EKIVEHKDAT EKEQRISEIN TGTYCFDNKA LFEALENVSN DNVQGEYYLP DVIKILKDSD EVVAAYRMES FEESLGVNDR IALAEASKLM QRRINENHMR NGVTLVNPES TYIDIDVKIG QDTVIEPGVM LRGKTVIGDD CVVTSGSEIV NSVIGERVHV RTSSIFESKV GDDVQIGPYA HLRPESDIHD HVKIGNYVET KKAVVGEGTK LPHFIYMGDA EIGKNVNVGC GSIAVNYDGK NKAKTIIGDN VFVGCNSNLI APVKVGDRAF IAAGSTITKD VPEDALGIAR AKQDNKLGYA KHLNHGK //