ID A0R8C1_BACAH Unreviewed; 465 AA. AC A0R8C1; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 11-SEP-2007, entry version 9. DE UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23). GN Name=gcaD; 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]. 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: Context: Lipopolysaccharide (LPS) biosynthesis; lipid A CC biosynthesis. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine CC biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from D- CC glucosamine 6-phosphate (route II): step 2/2. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine CC biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D- CC glucosamine 1-phosphate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; -; Genomic_DNA. DR GO; GO:0008415; F:acyltransferase activity; IEA:InterPro. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase act...; IEA:InterPro. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR InterPro; IPR005882; GlmU. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR005835; NTP_transferase. DR Pfam; PF00132; Hexapep; 6. DR Pfam; PF00483; NTP_transferase; 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. SQ SEQUENCE 465 AA; 50315 MW; 9743CFC3535E739F CRC64; MRWRVYMSNR FAVILAAGKG TRMKSKLYKV LHPVCGKPMV QHVVDQVSQL GLQKLVTVVG HGAEMVQEQL GNVSEFALQA EQLGTAHAVD QAAGVLANEE GTTLVICGDT PLITAETMEA LLQQHKEAGA MATVLTAYIE EPAGYGRIVR NENGHVEKIV EHKDANEKEL AIKEINTGTY CFDNKALFAS LSKVSNDNVQ GEYYLPDVIE ILKNEGHIVS AYQTEHFDET LGVNDRVALS QAEIIMKNRI NRKNMVNGVT IIDPSNTYIS ADAIIGSDTV LHPGTIIEGN TVIGSDCEIG PHTVIRDSEI GDRTTIRQST VHDSKLGTEV SVGPFAHIRP DSVIGDEVRV GNFVEIKKTV FGNRSKASHL SYIGDAQVGE DVNLGCGSIT VNYDGKNKFK TVIGNGVFIG CNSNLVAPVT VEDGAYVAAG STITENVPSK ALSVARARQV NKEDYVDQLL NKKKS //