ID GLMU_BACAH Reviewed; 459 AA. AC A0R8C1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 24-JAN-2024, entry version 102. 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}; OrderedLocusNames=BALH_0044; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/jb.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). 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; CC Evidence={ECO:0000255|HAMAP-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 -!- SEQUENCE CAUTION: CC Sequence=ABK83464.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; CP000485; ABK83464.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_000071032.1; NC_008600.1. DR AlphaFoldDB; A0R8C1; -. DR SMR; A0R8C1; -. DR GeneID; 45020089; -. DR KEGG; btl:BALH_0044; -. DR HOGENOM; CLU_029499_15_2_9; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000000761; 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; IPR005835; NTP_transferase_dom. 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; 3. DR Pfam; PF00483; NTP_transferase; 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; Repeat; Transferase. FT CHAIN 1..459 FT /note="Bifunctional protein GlmU" FT /id="PRO_0000337708" FT REGION 1..230 FT /note="Pyrophosphorylase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT REGION 231..251 FT /note="Linker" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT REGION 252..459 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT ACT_SITE 363 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 9..12 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 23 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 73 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 78..79 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 140 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 155 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 170 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 228 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 228 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 333 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 351 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 366 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 377 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..387 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 423 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" FT BINDING 440 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631" SQ SEQUENCE 459 AA; 49423 MW; 438E43713A39DA05 CRC64; MSNRFAVILA AGKGTRMKSK LYKVLHPVCG KPMVQHVVDQ VSQLGLQKLV TVVGHGAEMV QEQLGNVSEF ALQAEQLGTA HAVDQAAGVL ANEEGTTLVI CGDTPLITAE TMEALLQQHK EAGAMATVLT AYIEEPAGYG RIVRNENGHV EKIVEHKDAN EKELAIKEIN TGTYCFDNKA LFASLSKVSN DNVQGEYYLP DVIEILKNEG HIVSAYQTEH FDETLGVNDR VALSQAEIIM KNRINRKNMV NGVTIIDPSN TYISADAIIG SDTVLHPGTI IEGNTVIGSD CEIGPHTVIR DSEIGDRTTI RQSTVHDSKL GTEVSVGPFA HIRPDSVIGD EVRVGNFVEI KKTVFGNRSK ASHLSYIGDA QVGEDVNLGC GSITVNYDGK NKFKTVIGNG VFIGCNSNLV APVTVEDGAY VAAGSTITEN VPSKALSVAR ARQVNKEDYV DQLLNKKKS //