ID GLMU_BLOPB Reviewed; 462 AA. AC Q494C1; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 110. 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=BPEN_010; OS Blochmannia pennsylvanicus (strain BPEN). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; ant endosymbionts; Blochmannia. OX NCBI_TaxID=291272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BPEN; RX PubMed=16077009; DOI=10.1101/gr.3771305; RA Degnan P.H., Lazarus A.B., Wernegreen J.J.; RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel RT evolutionary trends among bacterial mutualists of insects."; RL Genome Res. 15:1023-1033(2005). CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- CC terminal domain catalyzes the transfer of acetyl group from acetyl CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- CC triphosphate), a reaction catalyzed by the N-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N- CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01631}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from CC 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. {ECO:0000255|HAMAP- CC Rule:MF_01631}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {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; CP000016; AAZ40660.1; -; Genomic_DNA. DR RefSeq; WP_011282566.1; NC_007292.1. DR AlphaFoldDB; Q494C1; -. DR SMR; Q494C1; -. DR STRING; 291272.BPEN_010; -. DR KEGG; bpn:BPEN_010; -. DR eggNOG; COG1207; Bacteria. DR HOGENOM; CLU_029499_15_2_6; -. DR OrthoDB; 9775031at2; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000007794; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule. 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. 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 CDD; cd02540; GT2_GlmU_N_bac; 1. DR CDD; cd03353; LbH_GlmU_C; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR038009; GlmU_C_LbH. 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_sf. DR NCBIfam; TIGR01173; glmU; 1. DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1. DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm; KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. FT CHAIN 1..462 FT /note="Bifunctional protein GlmU" FT /id="PRO_0000233739" FT REGION 1..235 FT /note="Pyrophosphorylase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT REGION 236..256 FT /note="Linker" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT REGION 257..462 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT ACT_SITE 369 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 11..14 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 25 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 80 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 85..86 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 107..109 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 109 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 144 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 159 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 233 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 339 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 357 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 372 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 383 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 386 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 392..393 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 429 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 446 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" SQ SEQUENCE 462 AA; 51550 MW; 9E857B19A26FCFD2 CRC64; MSYINFSAII LAAGRGNRML SDTPKVLYQI GGKFMLQHLI DSVMQVGVSS IYVVHGYKGE MIIKEINTNQ YKIPVYWILQ HDLTGTGDAV QRVLPFISDD EEVLVLYGDV PFVSYKTLQR LHVIKSQCDI SMLTATLPNP KGYGRIVRNQ EGSVVSIIEH DDIINDDQKK IKEVSTGIFI AISNHLKCWL STLTTHKSKN EFYLTDIIQI AHQSGYSIHT MCPDDTFEIM GVNSKSDFVD LDKQYQQRKV QCLLSSGLMI IDPNRFDLRG TLVHGKDVYI DINVIIEGHV SLGNRVKIGA SCILKDTIVA DDVEIYPFSI IENTTIGFQS KVGPFVRLRP GTELKEKSHV GNFVEIKNTR LGEQSKVKHL SYLGDAEIGN QVNIGAGTII CNYDGMMKHQ TIIGDDVFIG ADSQLVAPIT IGKNVTIGAG TTVTRDVAAN ETIISRIRQF SILNWKRLKN KK //