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 05-SEP-2012, entry version 47. DE RecName: Full=Bifunctional protein GlmU; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase; DE EC=2.7.7.23; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase; DE EC=2.3.1.157; GN Name=glmU; OrderedLocusNames=BALH_0044; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; 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-GlcNAc. Responsible for the CC acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl CC transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc (By CC similarity). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-D-glucosamine. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). 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 -!- 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 -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. CC -!- SEQUENCE CAUTION: CC Sequence=ABK83464.1; Type=Erroneous initiation; 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; YP_892971.1; NC_008600.1. DR ProteinModelPortal; A0R8C1; -. DR SMR; A0R8C1; 3-453. DR STRING; A0R8C1; -. DR EnsemblBacteria; EBBACT00000066931; EBBACP00000065168; EBBACG00000066922. DR GeneID; 4545824; -. DR GenomeReviews; CP000485_GR; BALH_0044. DR KEGG; btl:BALH_0044; -. DR PATRIC; 18992047; VBIBacThu63319_0126. DR eggNOG; COG1207; -. DR HOGENOM; HOG000283476; -. DR KO; K04042; -. DR ProtClustDB; PRK14354; -. DR BioCyc; BTHU412694:BALH_0044-MONOMER; -. DR UniPathway; UPA00113; UER00532. 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:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:EC. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR GO; GO:0007047; P:cellular 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-KW. 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 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; IPR011004; Trimer_LpxA-like. DR PANTHER; PTHR22572:SF17; PTHR22572:SF17; 1. DR Pfam; PF00132; Hexapep; 4. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; Trimer_LpxA_like; 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 (By similarity). FT REGION 9 12 Substrate binding (By similarity). FT REGION 78 79 Substrate binding (By similarity). FT REGION 231 251 Linker (By similarity). FT REGION 252 459 N-acetyltransferase (By similarity). FT ACT_SITE 363 363 Proton acceptor (By similarity). FT METAL 103 103 Magnesium (By similarity). FT METAL 228 228 Magnesium (By similarity). FT BINDING 73 73 Substrate (By similarity). FT BINDING 140 140 Substrate; via amide nitrogen (By FT similarity). FT BINDING 155 155 Substrate (By similarity). FT BINDING 170 170 Substrate (By similarity). FT BINDING 387 387 Acetyl-CoA (By similarity). FT BINDING 423 423 Acetyl-CoA; via amide nitrogen (By FT similarity). FT BINDING 440 440 Acetyl-CoA (By similarity). 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 //