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 08-MAY-2019, entry version 84. 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=BALH_0044; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; 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., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P., RA Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., RA Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., RA Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., RA 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 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: CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) CC + N-acetyl-alpha-D-glucosamine 1-phosphate; CC Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; CC EC=2.3.1.157; 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; CC Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; CC EC=2.7.7.23; 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- 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 -!- SEQUENCE CAUTION: CC Sequence=ABK83464.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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 SMR; A0R8C1; -. DR PRIDE; A0R8C1; -. DR EnsemblBacteria; ABK83464; ABK83464; BALH_0044. DR KEGG; btl:BALH_0044; -. DR HOGENOM; HOG000283476; -. DR KO; K04042; -. 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:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. 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; cd03353; LbH_GlmU_C; 1. DR Gene3D; 3.90.550.10; -; 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 Pfam; PF00132; Hexapep; 3. 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; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Repeat; Transferase. FT CHAIN 1 459 Bifunctional protein GlmU. FT /FTId=PRO_0000337708. FT REGION 1 230 Pyrophosphorylase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 9 12 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 78 79 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 231 251 Linker. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 252 459 N-acetyltransferase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 386 387 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 363 363 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 103 103 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 228 228 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 23 23 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 73 73 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 140 140 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 155 155 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 170 170 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 228 228 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 333 333 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 351 351 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 366 366 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 377 377 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 423 423 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 440 440 Acetyl-CoA. {ECO:0000255|HAMAP- FT 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 //