ID T2T4J8_HELPX Unreviewed; 433 AA. AC T2T4J8; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-OCT-2020, entry version 42. 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 ECO:0000313|EMBL:EQD99495.1}; GN ORFNames=L931_03335 {ECO:0000313|EMBL:EQD99495.1}; OS Helicobacter pylori PZ5024. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=1337391 {ECO:0000313|EMBL:EQD99495.1, ECO:0000313|Proteomes:UP000015645}; RN [1] {ECO:0000313|EMBL:EQD99495.1, ECO:0000313|Proteomes:UP000015645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PZ5024 {ECO:0000313|EMBL:EQD99495.1, RC ECO:0000313|Proteomes:UP000015645}; RX PubMed=24051318; RA Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.; RT "Draft Genome Sequences of Helicobacter pylori Strains Isolated from RT Regions of Low and High Gastric Cancer Risk in Colombia."; RL Genome Announc. 1:e00736-13(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:EQD99495.1}. 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; ASYS01000042; EQD99495.1; -; Genomic_DNA. DR RefSeq; WP_021171689.1; NZ_ASYS01000042.1. DR EnsemblBacteria; EQD99495; EQD99495; L931_03335. DR PATRIC; fig|1337391.3.peg.240; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000015645; 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; IPR018357; Hexapep_transf_CS. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR Pfam; PF14602; Hexapep_2; 1. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01631, ECO:0000313|EMBL:EQD99495.1}; 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}; Coiled coil {ECO:0000256|SAM:Coils}; 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:EQD99495.1}. FT DOMAIN 4..129 FT /note="NTP_transf_3" FT /evidence="ECO:0000259|Pfam:PF12804" FT REGION 1..226 FT /note="Pyrophosphorylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 7..10 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 80..81 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 227..247 FT /note="Linker" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 248..433 FT /note="N-acetyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 362..363 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT COILED 223..243 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 339 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 106 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 224 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 21 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 138 FT /note="UDP-GlcNAc; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 152 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 167 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 224 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 311 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 328 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 353 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 356 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 381 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 399 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 416 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" SQ SEQUENCE 433 AA; 47876 MW; 93E295DE420B15EE CRC64; MLSVIILAAG KGTRMHSSLP KTLHTICGEP MLFYILEVAF SISDDVHLIL HHQQERIKEV VSKRFKGVIF HAQIVEKYSG TGGAIMQEDK TPIPTQHERV LILNADMPLI TKDALTPLLE SQNNAIGLLH LADPKGYGRV VLENHHVKKI VEEKDANNEE KTIKSVNAGV YFFERKFLER YLPKLNDQNA QKEYYLTDLI ALGIKGNEKI DAIFLEEECF LGVNSQTERA KAEEIMLERL RKNAMDSGVM MQLPNSIYLE KGVSFKGECV LEQGVRLIGN CLIENARIKA YSVIEESQII NSSVGPFAHA RPKSVICDSH VGNFVETKNA KLQGAKAGHL SYLGDCEIGK NTNIGAGVIT CNYDGKKKHQ TIIGENVFIG SDSQLVAPIN IGSNVLIGSG TTITKDIPSG SLSLSRAPQT NIENGYFKFF KKP //