ID C8KFW0_LISMN Unreviewed; 457 AA. AC C8KFW0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 04-FEB-2015, entry version 25. DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083647}; GN Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631}; GN ORFNames=LMMG_02757 {ECO:0000313|EMBL:EEW23514.1}; OS Listeria monocytogenes F6900. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=393128 {ECO:0000313|EMBL:EEW23514.1}; RN [1] {ECO:0000313|EMBL:EEW23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F6900 {ECO:0000313|EMBL:EEW23514.1}; 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-N-acetylglucosamine (UDP- CC GlcNAc). The C-terminal domain catalyzes the transfer of acetyl CC group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) CC to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is CC converted into UDP-GlcNAc by the transfer of uridine 5- CC monophosphate (from uridine 5-triphosphate), a reaction catalyzed CC by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083685}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083699}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083568}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01631}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083707}. 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 {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083673}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083576}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083712}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW23514.1}. 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 EnsemblBacteria; EEW23514; EEW23514; LMMG_02757. DR PATRIC; 27483816; VBILisMon69349_2864. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.550.10; -; 1. 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; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 4. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083661}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083584}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083688}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083649}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083580}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083557}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083642}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083639}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083721}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083725}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083632}. FT REGION 1 230 Pyrophosphorylase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 9 12 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 78 79 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 231 251 Linker. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT REGION 252 457 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 386 387 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 363 363 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 103 103 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 228 228 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 23 23 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 73 73 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 140 140 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 155 155 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 170 170 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 228 228 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 333 333 Acetyl-CoA; amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 351 351 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 366 366 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 377 377 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 423 423 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 440 440 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. 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 //