ID A0A4U0QHK2_9RHOB Unreviewed; 447 AA. AC A0A4U0QHK2; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 12-AUG-2020, entry version 6. 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:TJZ80770.1}; GN ORFNames=FA740_16770 {ECO:0000313|EMBL:TJZ80770.1}; OS Paracoccus hibiscisoli. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=2023261 {ECO:0000313|EMBL:TJZ80770.1, ECO:0000313|Proteomes:UP000306223}; RN [1] {ECO:0000313|EMBL:TJZ80770.1, ECO:0000313|Proteomes:UP000306223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCTCC AB2016182 {ECO:0000313|EMBL:TJZ80770.1, RC ECO:0000313|Proteomes:UP000306223}; RA Li J.; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. 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: 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:TJZ80770.1}. 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; SUNH01000032; TJZ80770.1; -; Genomic_DNA. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000306223; 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; 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. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 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, ECO:0000313|EMBL:TJZ80770.1}; 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:TJZ80770.1}. FT DOMAIN 8..142 FT /note="NTP_transf_3" FT /evidence="ECO:0000259|Pfam:PF12804" FT REGION 1..229 FT /note="Pyrophosphorylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 11..14 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 83..84 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 106..108 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 230..250 FT /note="Linker" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 251..447 FT /note="N-acetyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 369..370 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT ACT_SITE 346 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 108 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 227 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 25 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 78 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 141 FT /note="UDP-GlcNAc; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 155 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 170 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 227 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 316 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 334 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 349 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 363 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 388 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 406 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 423 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" SQ SEQUENCE 447 AA; 46673 MW; 23256353ED2BD24B CRC64; MSENAVGVVI LAAGQGSRMQ SDLPKVLHRL GGVPLVGHAL RAARSLEPEQ IVVVTGHGTQ AVTAAVARLD PDAACVLQAE QLGTGHAVRQ ALPALEGFEG RVIVLYGDTP FIAEETLAEL AAHPADLVVL GFEAEEPGRY GRLVVTDRGL ERIVEWKDAD AATRDIALCN SGVMALSADL LRRLIAGLSN QNASGEYYLT DLVALARAEG RRADVVICPE AETLGINTRI ELAAAEAAFQ ARARARLMED GVTLTDPGSV FLALDTVIGR DAVIGPNVVF GPGVTVESGA EILPFCHLEG CHVSEGATVG PFARLRPGAE LGTDVHVGNF VEIKNAVLDE GVKVGHLTYL GDAHVGEHTN IGAGTITCNY DGVSKHRTTI GARAFIGSDT MLVAPVRVGA DAMTGSGSVI TEDIPDGALA IGRARQATKP GLALRLMAAL RLKKEAR //