ID A0A396MLM5_9CLOT Unreviewed; 415 AA. AC A0A396MLM5; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 13-NOV-2019, entry version 4. DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|SAAS:SAAS01076914}; GN Name=glmU {ECO:0000313|EMBL:RHS35519.1}; GN ORFNames=DWV55_07915 {ECO:0000313|EMBL:RHS35519.1}; OS Butyricicoccus sp. AF10-3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Butyricicoccus; unclassified Butyricicoccus. OX NCBI_TaxID=2292196 {ECO:0000313|EMBL:RHS35519.1, ECO:0000313|Proteomes:UP000266580}; RN [1] {ECO:0000313|EMBL:RHS35519.1, ECO:0000313|Proteomes:UP000266580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF10-3 {ECO:0000313|EMBL:RHS35519.1, RC ECO:0000313|Proteomes:UP000266580}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut RT microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|SAAS:SAAS01076924}. 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:0000256|SAAS:SAAS01115178}; 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:0000256|SAAS:SAAS01115154}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS01076930}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000256|SAAS:SAAS01076917}. 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:0000256|SAAS:SAAS01076916}. 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:0000256|SAAS:SAAS01076929}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|SAAS:SAAS01076913}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01076942}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|SAAS:SAAS01076912}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000256|SAAS:SAAS01076943}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RHS35519.1}. 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; QUHS01000013; RHS35519.1; -; Genomic_DNA. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000266580; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC. 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-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 CDD; cd03353; LbH_GlmU_C; 1. DR InterPro; IPR038009; GlmU_C_LbH. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR Pfam; PF00132; Hexapep; 3. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|SAAS:SAAS01076923}; KW Cell shape {ECO:0000256|SAAS:SAAS01076918}; KW Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS01076915}; KW Complete proteome {ECO:0000313|Proteomes:UP000266580}; KW Cytoplasm {ECO:0000256|SAAS:SAAS01076925}; KW Magnesium {ECO:0000256|SAAS:SAAS01076919}; KW Metal-binding {ECO:0000256|SAAS:SAAS01076921}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS01076922}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01076928}; KW Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS01076926}; KW Repeat {ECO:0000256|SAAS:SAAS01076927}; KW Transferase {ECO:0000256|SAAS:SAAS01076941, KW ECO:0000313|EMBL:RHS35519.1}. SQ SEQUENCE 415 AA; 43586 MW; B87E86D996EE880A CRC64; MNKVNAVMVG GLFDESGISA FARPVLFGTA GDAMRDALPD AVEACFFAHD DREPAVAGAQ DIALDAANRF ASLAALPESE HVLVLAAPFA LAEEDALFHL AETHLNTGYG VSVLSAEQQG FDAEGQPLPR DSRCYAAMFT WDMLKKALAS GADTLDGLVA AAVAAGAQKG IAITNKIYVI CDGTAAFMAQ VEMMQRVNFG LIKKGVQIFD LTSTYIAPDA DIAPGATILP GCHIRPGCKV GAGAVIGPNT ILEKAEIGAG TTVNNSQVYE STVGSNTTVG PFAYIRPQSV VGDGCRIGDF VELKKSTIGN GTKVSHLTYI GDATVGERVN FGCGTVVVNY DGYHKYRTEI GDDCFIGCNT NLVSPVKLGD RAFTAAGTTV TKDVPAGALS VARARQTNLE GWNDRRRAAH EKDKK //