ID M2Z934_9PSEU Unreviewed; 495 AA. AC M2Z934; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 12-AUG-2020, entry version 45. DE RecName: Full=Bifunctional protein GlmU {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}; 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}; 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 44594T."; RL Genome Announc. 1:E0013813-E0013813(2013). 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|HAMAP-Rule:MF_01631}. 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|HAMAP-Rule:MF_01631}; 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|HAMAP-Rule:MF_01631}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01631}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01631}. 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|HAMAP-Rule:MF_01631}. 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. {ECO:0000256|HAMAP- CC Rule:MF_01631}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000256|ARBA:ARBA00007707, CC 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|ARBA:ARBA00007947, ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 EnsemblBacteria; EME63792; EME63792; H074_04224. DR PATRIC; fig|1284240.4.peg.848; -. 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-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule. 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-UniRule. 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 CDD; cd03353; LbH_GlmU_C; 1. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR038009; GlmU_C_LbH. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like_sf. 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|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01631}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_01631}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_01631}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01631}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01631}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01631}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01631}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01631}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_01631}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01631}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01631, ECO:0000313|EMBL:EME63792.1}. FT DOMAIN 8..144 FT /note="NTP_transf_3" FT /evidence="ECO:0000259|Pfam:PF12804" FT REGION 1..239 FT /note="Pyrophosphorylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 10..13 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 86..87 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 110..112 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 240..260 FT /note="Linker" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 261..495 FT /note="N-acetyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 395..396 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 455..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 476..495 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 372 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 112 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 237 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 24 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 81 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 149 FT /note="UDP-GlcNAc; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 164 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 179 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 237 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 342 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 360 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 375 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 386 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 432 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="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 //