ID M2Z934_9PSEU Unreviewed; 495 AA. AC M2Z934; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 10-MAY-2017, entry version 29. DE RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631}; DE EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631}; DE EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631}; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631}; GN Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631}; GN ORFNames=H074_04224 {ECO:0000313|EMBL:EME63792.1}; OS Amycolatopsis decaplanina DSM 44594. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Amycolatopsis. OX NCBI_TaxID=1284240 {ECO:0000313|EMBL:EME63792.1, ECO:0000313|Proteomes:UP000054226}; RN [1] {ECO:0000313|EMBL:EME63792.1, ECO:0000313|Proteomes:UP000054226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44594 {ECO:0000313|EMBL:EME63792.1, RC ECO:0000313|Proteomes:UP000054226}; RX PubMed=23558534; RA Kaur N., Kumar S., Bala M., Raghava G.P., Mayilraj S.; RT "Draft Genome Sequence of Amycolatopsis decaplanina Strain DSM RT 44594T."; RL Genome Announc. 1:E0013813-E0013813(2013). 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:SAAS00650355}. 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:SAAS00650344}. 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:SAAS00650293}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01631}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00650347}. 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:SAAS00650354}. 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:SAAS00650342}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00650301}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00650327}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00650305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00650312}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}. 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:EME63792.1}. 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; AOHO01000026; EME63792.1; -; Genomic_DNA. DR RefSeq; WP_007028783.1; NZ_AOHO01000026.1. DR RefSeq; WP_007028783.1; NZ_AOHO01000026.1. DR RefSeq; WP_007028783.1; NZ_AOHO01000026.1. DR EnsemblBacteria; EME63792; EME63792; H074_04224. DR OrthoDB; POG091H02I2; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000054226; 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-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; 1. 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:SAAS00650319}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650332}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650295}; KW Complete proteome {ECO:0000313|Proteomes:UP000054226}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650352}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650323}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650321}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650297}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650324}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650358}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650299}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00650328, ECO:0000313|EMBL:EME63792.1}. FT DOMAIN 8 144 NTP_transf_3. {ECO:0000259|Pfam:PF12804}. FT REGION 1 239 Pyrophosphorylase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 10 13 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 86 87 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 110 112 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 240 260 Linker. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT REGION 261 495 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 395 396 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 372 372 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 112 112 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 237 237 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 24 24 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 81 81 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 149 149 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 164 164 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 179 179 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 237 237 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 342 342 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 360 360 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 375 375 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 386 386 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 432 432 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. SQ SEQUENCE 495 AA; 50761 MW; BC243CB5A1E19949 CRC64; MTGPLSTLIL AAGEGTRMRS STPKVLHPIA GRPLVEHAVR AAAGLNPEHL VVVIGHGRDS VGARLAKVGE ALGREVVTAV QEEQKGTGHA VSCALSALPA GLTGTVVVSY GDVPLLDTET LASLVAEHTS TGNAVTVLTA VVEDPTGYGR IIRDENGVVT SIVEQKDATP EQHEIAEINS GVYAFDASVL VDGLSRLSTD NAQGELYLTD VLGIARGDGK GVGALVIDDP WVTEGVNDRV QLSVLGAELN RRIVRGWQRA GVTVVDPAST WIDAGVTLSR DVVIEPGVQL KGSTSVGEGT QIGPDSTLEN VSVGAGASVV RTHGSDSELG DGVKVGPFTY LRPGSKLGAK GKLGAFVETK NADIGAGTKV PHLTYVGDAT IGENSNIGCS SVFVNYDGVN KHHTTIGSHV RLGADNTFVA PVTIGDGAYS GAGTVIRQDV PPGALAVSTG PQRNIEDWVS RRRPGTPAAE AASAAKQDTT AVSDSNKGND GESPA //