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 16-SEP-2015, entry version 61. DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631}; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631}; GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; GN 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]. 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-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:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01631}; 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 {ECO:0000255|HAMAP-Rule:MF_01631}. 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:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}. 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; WP_011961493.1; NC_009524.1. DR ProteinModelPortal; A5WHT0; -. DR STRING; 349106.PsycPRwf_2281; -. DR EnsemblBacteria; ABQ95221; ABQ95221; PsycPRwf_2281. DR KEGG; prw:PsycPRwf_2281; -. DR eggNOG; COG1207; -. DR HOGENOM; HOG000283476; -. DR KO; K04042; -. DR OMA; FAHARPK; -. DR OrthoDB; EOG6Z6FQZ; -. DR BioCyc; PPRW349106:GHZF-2351-MONOMER; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000001993; Chromosome. 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. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 2. DR Pfam; PF14602; Hexapep_2; 1. DR Pfam; PF12804; NTP_transf_3; 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; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. FT CHAIN 1 455 Bifunctional protein GlmU. FT /FTId=PRO_1000073649. FT REGION 1 228 Pyrophosphorylase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 10 13 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 80 81 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 102 104 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 229 249 Linker. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 250 455 N-acetyltransferase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 385 386 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 362 362 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 104 104 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 226 226 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 24 24 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 75 75 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 138 138 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 153 153 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 168 168 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 226 226 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 332 332 Acetyl-CoA; amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 350 350 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 365 365 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 376 376 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 422 422 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 439 439 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. 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 //