ID A0A5P5ZH93_9LACO Unreviewed; 461 AA. AC A0A5P5ZH93; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 07-OCT-2020, entry version 4. DE SubName: Full=Bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU {ECO:0000313|EMBL:QFG50779.1}; DE EC=2.3.1.157 {ECO:0000313|EMBL:QFG50779.1}; DE EC=2.7.7.23 {ECO:0000313|EMBL:QFG50779.1}; 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000256|ARBA:ARBA00007947}. 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 Proteomes; UP000325393; Chromosome. 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:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR GO; GO:0071555; P: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: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:InterPro. 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|ARBA:ARBA00023315, KW ECO:0000313|EMBL:QFG50779.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000313|EMBL:QFG50779.1}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, 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 //