ID F8IJN0_ALIAT Unreviewed; 470 AA. AC F8IJN0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 05-SEP-2012, entry version 7. DE RecName: Full=Bifunctional protein GlmU; GN Name=glmU; OrderedLocusNames=TC41_0245; OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus OS acidocaldarius). OC Bacteria; Firmicutes; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=1048834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tc-4-1; RA Chen Y., He Y., Dong Z., Hu S.; RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. RT Tc-4-1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. 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: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. 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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. 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; CP002902; AEJ42219.1; -; Genomic_DNA. DR RefSeq; YP_005516738.1; NC_017167.1. DR GeneID; 12107156; -. DR KEGG; aad:TC41_0245; -. DR KO; K04042; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:HAMAP. DR GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_01631; GlmU; 1; -. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR025877; MobA-like_NTP_Trfase_dom. DR InterPro; IPR011004; Trimer_LpxA-like. DR PANTHER; PTHR22572:SF17; PTHR22572:SF17; 1. DR Pfam; PF00132; Hexapep; 3. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF51161; Trimer_LpxA_like; 1. DR TIGRFAMs; TIGR01173; GlmU; 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 REGION 1 229 Pyrophosphorylase (By similarity). FT REGION 8 11 Substrate binding (By similarity). FT REGION 77 78 Substrate binding (By similarity). FT REGION 230 250 Linker (By similarity). FT REGION 251 470 N-acetyltransferase (By similarity). FT ACT_SITE 362 362 Proton acceptor (By similarity). FT METAL 102 102 Magnesium (By similarity). FT METAL 227 227 Magnesium (By similarity). FT BINDING 72 72 Substrate (By similarity). FT BINDING 139 139 Substrate; via amide nitrogen (By FT similarity). FT BINDING 154 154 Substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 386 386 Acetyl-CoA (By similarity). FT BINDING 404 404 Acetyl-CoA (By similarity). FT BINDING 422 422 Acetyl-CoA; via amide nitrogen (By FT similarity). FT BINDING 439 439 Acetyl-CoA (By similarity). SQ SEQUENCE 470 AA; 51294 MW; 4E3529CBA034477C CRC64; MAQTAVVLAA GHGTRMKSQT HKVLHPVCGK PMIHHLLDSL REARMDQVVV VVGQHREQVE AAIRGRAEIA VQEKQLGTAD AVRAALPLVP SDTETVVVLY GDAPLIRPET ILHLMRLREE TRAACVVLAA EVTNPKGLGR VFLNDRGEVE RIVEEKDATP EERAHRLINT GIYAFRRDAL EEALREVKND NAQGEYYLTD TALILSRRGE RVIAHIAEDE DEIASVNNRA ELARVEAICR QRILARWMME GVTVVDPNAT YIEADVELAP DVTLLPGTML AGRTRISTGA VIGPHTRLVN TVVREGARVQ FTVAVEAVIG EEAEVGPFAY LRPGAEIGRR VKIGDFVEVK NSRIGDDTKV SHLAYVGDAE IGRNVNIGCG AITVNYDGER KHRTVIGDDS FVGSNVNLIA PVTIGKGAYV VAGTTVTDDV GDDGFAIGRV PQTTKPNYVR AWKARRQNRN PEKGGNHCGH //