ID A0A0B5D1Z6_9CORY Unreviewed; 492 AA. AC A0A0B5D1Z6; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 29-APR-2015, entry version 2. DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|SAAS:SAAS00083647}; GN Name=glmU {ECO:0000313|EMBL:AJE32696.1}; GN ORFNames=B842_04215 {ECO:0000313|EMBL:AJE32696.1}; OS Corynebacterium humireducens NBRC 106098 = DSM 45392. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE32696.1, ECO:0000313|Proteomes:UP000031524}; RN [1] {ECO:0000313|EMBL:AJE32696.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 45392 {ECO:0000313|EMBL:AJE32696.1}; 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|SAAS:SAAS00083685}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {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|SAAS:SAAS00083568}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00172548}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000256|SAAS:SAAS00172548}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {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|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:SAAS00083578}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00083712}. 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 UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000031524; Chromosome. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.550.10; -; 1. 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; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 4. 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|SAAS:SAAS00083661, KW ECO:0000313|EMBL:AJE32696.1}; KW Cell shape {ECO:0000256|SAAS:SAAS00083584}; KW Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00083688}; KW Complete proteome {ECO:0000313|Proteomes:UP000031524}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00083649}; KW Magnesium {ECO:0000256|SAAS:SAAS00083580}; KW Metal-binding {ECO:0000256|SAAS:SAAS00083557}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00083642}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00083639}; KW Peptidoglycan synthesis {ECO:0000256|SAAS:SAAS00083721}; KW Repeat {ECO:0000256|SAAS:SAAS00083725}; KW Transferase {ECO:0000256|SAAS:SAAS00083632, KW ECO:0000313|EMBL:AJE32696.1}. 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 //