ID A0A3S4KW49_AVIVO Unreviewed; 456 AA. AC A0A3S4KW49; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 05-JUN-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:VEB22381.1}; GN ORFNames=NCTC3438_00420 {ECO:0000313|EMBL:VEB22381.1}; OS Avibacterium volantium (Pasteurella volantium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Avibacterium. OX NCBI_TaxID=762 {ECO:0000313|EMBL:VEB22381.1, ECO:0000313|Proteomes:UP000268198}; RN [1] {ECO:0000313|EMBL:VEB22381.1, ECO:0000313|Proteomes:UP000268198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC3438 {ECO:0000313|EMBL:VEB22381.1, RC ECO:0000313|Proteomes:UP000268198}; RG Pathogen Informatics; RL Submitted (DEC-2018) 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 --------------------------------------------------------------------------- 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; LR134167; VEB22381.1; -; Genomic_DNA. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000268198; Chromosome 1. 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; 4. 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 Complete proteome {ECO:0000313|Proteomes:UP000268198}; 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}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458685}; KW Reference proteome {ECO:0000313|Proteomes:UP000268198}; 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}. FT DOMAIN 6 128 NTP_transf_3. {ECO:0000259|Pfam:PF12804}. FT REGION 1 227 Pyrophosphorylase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 9 12 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 79 80 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 101 103 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 228 248 Linker. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT REGION 249 456 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 384 385 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 361 361 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 103 103 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 225 225 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 23 23 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 74 74 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 138 138 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 152 152 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 167 167 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 225 225 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 331 331 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 349 349 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 364 364 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 375 375 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 378 378 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 403 403 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 421 421 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 438 438 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. SQ SEQUENCE 456 AA; 49532 MW; 4BCBD0F71BBCD704 CRC64; MKNLSVVILA AGKGTRMYSD LPKVLHKVAG KPMVKHVIDT AKQLNADNIH LIYGHGAELL QQHLADENVN WVLQPVQLGT GHAMQQAAPF FADDENIVML YGDAPLITAQ TLQKLIDAKP ENGIALLTAH LDDPTGYGRI IRQDGNVVAI VEQKDATPEQ LAIQEVNTGV MVSSGASFRK WLAKLDNNNA QGEYYMTDVI KFANQDGCKV AAVQAQDLME VEGANNRLQL AELERYYQRK QAEKLLLAGV SLRDPSRFDL RGEILHGKDV EIDVNVIIEG NVKLGDRVKI GAGCIIKDCV IGDDVEIKPY SVFEDAVIGE QAQIGPFSRL RPGTELAAQT HIGNFVEVKK SHIGKGSKVN HLSYVGDSEI GANCNIGAGT ITCNYDGVNK FKTVIGDDVF VGSDSQLVAP VTIAKGATIG AGTTVTKDIA ENELVISRVP QRNIQGWKRP EKLEKK //