ID A0A5P5ZH93_9LACO Unreviewed; 461 AA. AC A0A5P5ZH93; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 17-JUN-2020, entry version 2. DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|SAAS:SAAS00083647}; GN Name=glmU {ECO:0000313|EMBL:QFG50779.1}; GN ORFNames=LA749_01510 {ECO:0000313|EMBL:QFG50779.1}; OS Lactobacillus acetotolerans. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1600 {ECO:0000313|EMBL:QFG50779.1, ECO:0000313|Proteomes:UP000325393}; RN [1] {ECO:0000313|EMBL:QFG50779.1, ECO:0000313|Proteomes:UP000325393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LA749 {ECO:0000313|EMBL:QFG50779.1, RC ECO:0000313|Proteomes:UP000325393}; RA Kim K.; RT "Genome sequencing of Lactobacillus acetotolerans."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- CC terminal domain catalyzes the transfer of acetyl group from acetyl CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- CC triphosphate), a reaction catalyzed by the N-terminal domain. CC {ECO:0000256|SAAS:SAAS00381483}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23; CC Evidence={ECO:0000256|SAAS:SAAS01124206}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N- CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; CC Evidence={ECO:0000256|SAAS:SAAS01124218}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00611499}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {ECO:0000256|SAAS:SAAS00083707}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from CC alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC {ECO:0000256|SAAS:SAAS00083565}. 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:SAAS00083673}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|SAAS:SAAS00569615}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00083712}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|SAAS:SAAS00569628}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000256|SAAS:SAAS00569629}. 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; CP044496; QFG50779.1; -; Genomic_DNA. DR RefSeq; WP_056970803.1; NZ_CP044496.1. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000325393; Chromosome. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC. DR CDD; cd03353; LbH_GlmU_C; 1. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR038009; GlmU_C_LbH. DR InterPro; IPR001451; Hexapep. 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. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|SAAS:SAAS00458646, KW ECO:0000313|EMBL:QFG50779.1}; Cell shape {ECO:0000256|SAAS:SAAS00083584}; KW Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00458644}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00458650}; KW Magnesium {ECO:0000256|SAAS:SAAS00458735}; KW Metal-binding {ECO:0000256|SAAS:SAAS00458606}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00083642}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00458661, KW ECO:0000313|EMBL:QFG50779.1}; KW Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00458685}; KW Repeat {ECO:0000256|SAAS:SAAS00458660}; KW Transferase {ECO:0000256|SAAS:SAAS00458747, ECO:0000313|EMBL:QFG50779.1}. FT DOMAIN 6..219 FT /note="NTP_transferase" FT /evidence="ECO:0000259|Pfam:PF00483" SQ SEQUENCE 461 AA; 50176 MW; B726C0D440FA255C CRC64; MKKFVVILAA GKGTRMKSKL YKVLHKVCGK TMVEHVVDAA QGVKPDKIIT VVGSGAGKVE KVLSGKSEFA FQEKQLGTGD AVLTTKDILG DKDGATLVIT GDTPLFTTET FQNLFAYHAK KGNAATVLTA EAPDPYGYGR IIRDEQGNVL RIVEQKDGKP EELEIKEINT GVFCFDNKKL FEALKHVDND NAQGEYYLTD VLEILRNKGE RVGAYKMPDF SESLGVNDRI ALAQATKIMQ KRINRNHMCD GVSFVDPTTA YIDSDVKIGN DTVIEGNVVI EGNTEIGSDC HITSGSRIVD SKIGNNVTIT SSTLQEAEMD DDTDIGPNSH LRPNAVIRKG AHVGNFVEIK NSEIGENTKV GHLTYVGDAT LGKDINVGCG TIFSNYDGVK KFHTNVGDHS FVGAGVTLIA PINVADHSFI AADSTITKNV GKYDMAIARG RQTNKPDYWH KLPLSHDKDW Q //