ID A0A0B5D1Z6_9CORY Unreviewed; 492 AA. AC A0A0B5D1Z6; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 16-MAR-2016, entry version 10. DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083647}; GN Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631, GN ECO:0000313|EMBL:AJE32696.1}; GN ORFNames=B842_04215 {ECO:0000313|EMBL:AJE32696.1}; OS Corynebacterium humireducens NBRC 106098 = DSM 45392. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE32696.1, ECO:0000313|Proteomes:UP000031524}; RN [1] {ECO:0000313|EMBL:AJE32696.1, ECO:0000313|Proteomes:UP000031524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524}; RA Ruckert C., Albersmeier A., Kalinowski J.; RT "Complete genome sequence of Corynebacterium humireducens DSM RT 45392(T), isolated from a wastewater-fed microbial fuel cell."; RL Submitted (APR-2013) 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|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00381483}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083699}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083568}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01631, ECO:0000256|SAAS:SAAS00242944}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01631, ECO:0000256|SAAS:SAAS00242944}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631, 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 CC from alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC {ECO:0000256|HAMAP-Rule:MF_01631, 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|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083673}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083578}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083712}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_01631}. 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; CP005286; AJE32696.1; -; Genomic_DNA. DR RefSeq; WP_040085384.1; NZ_CP005286.1. DR EnsemblBacteria; AJE32696; AJE32696; B842_04215. DR KEGG; chm:B842_04215; -. DR KO; K04042; -. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000031524; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-HAMAP. 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:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. 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 Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 3. DR Pfam; PF12804; NTP_transf_3; 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|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458646, ECO:0000313|EMBL:AJE32696.1}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458688}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458644}; KW Complete proteome {ECO:0000313|Proteomes:UP000031524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458650}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458735}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458606}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458631}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458661}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458685}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458660}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458747, ECO:0000313|EMBL:AJE32696.1}. FT DOMAIN 9 142 NTP_transf_3. {ECO:0000259|Pfam:PF12804}. FT REGION 1 240 Pyrophosphorylase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 12 15 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 88 89 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 241 261 Linker. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT REGION 262 492 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 396 397 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 373 373 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 113 113 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 238 238 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 26 26 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 83 83 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 150 150 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 165 165 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 180 180 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 238 238 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 343 343 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 361 361 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 376 376 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 387 387 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 390 390 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 415 415 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 433 433 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. SQ SEQUENCE 492 AA; 51030 MW; 35A76840446027A0 CRC64; MPQKNRCAVV VLAAGAGTRM KSAKQKTLHE IGGRTLLSHA LHAAAGVDPE HIVAVIGHQR DQVAPATEAV AAELGREVLQ AVQEEQNGTG HAVQCGLTPI PDFDGTVLVT NGDVPLLTPE TLRALLEAHT ASPTAVTVLS MRLDDPTGYG RIVRDDAGEV TAIVEQKDAT PEVLEIDEVN SGVFAFDGAL LRDALTKLDT DNAQGELYIT DVLGIAREAG HTVRAHVAAD PRELAGVNDR VQLAEAGREL NRRTVEAAMR GGATVIDPAS TFIGVNVTVG QDVVIHPGTQ LWGATSIGDN AVIGPDTTLT DMTVGRGASV IRTHGERSVI GENASVGPYT YIRPNTVLGE NGKLGGFVEA KNATIGRGSK VPHLTYIGDA TVGEESNIGA SSVFVNYDGV TKHHTTIGSH VRTGSDTMFI APVTVGDGAY SGAGTVIRED VPPGALAVSG GPQRTIEGWV ERKRPGSPAA EAAAAARAAG ESENDNATNQ EG //