ID A0A4U0QHK2_9RHOB Unreviewed; 447 AA. AC A0A4U0QHK2; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. 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}; RN [1] {ECO:0000313|EMBL:TJZ80770.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCTCC AB2016182 {ECO:0000313|EMBL:TJZ80770.1}; RA Li J.; RL Submitted (APR-2019) 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|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00381483}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; CC Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; CC EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS01124206}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) CC + N-acetyl-alpha-D-glucosamine 1-phosphate; CC Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; CC EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS01124218}; 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: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|HAMAP-Rule:MF_01631, 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|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00083673}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00569615}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, CC ECO:0000256|SAAS:SAAS00083712}. 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:SAAS00569628}. 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:SAAS00569629}. 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: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 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: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|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458646}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083584}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458644}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458650}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458735}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458606}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00083642}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458661, ECO:0000313|EMBL:TJZ80770.1}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458685}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458660}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458747, ECO:0000313|EMBL:TJZ80770.1}. FT DOMAIN 8 142 NTP_transf_3. {ECO:0000259|Pfam:PF12804}. FT REGION 1 229 Pyrophosphorylase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 11 14 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 83 84 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 106 108 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 230 250 Linker. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT REGION 251 447 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 369 370 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 346 346 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 108 108 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 227 227 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 25 25 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 78 78 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 141 141 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 155 155 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 170 170 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 227 227 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 316 316 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 334 334 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 349 349 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 360 360 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 363 363 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 388 388 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 406 406 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 423 423 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT 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 //