ID A0A5E5PLF6_9GAMM Unreviewed; 452 AA. AC A0A5E5PLF6; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 12-AUG-2020, entry version 5. 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=BPUTSESOX_1205 {ECO:0000313|EMBL:VVH50579.1}; OS uncultured Gammaproteobacteria bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples. OX NCBI_TaxID=86473 {ECO:0000313|EMBL:VVH50579.1}; RN [1] {ECO:0000313|EMBL:VVH50579.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Gfbio:bputsym:c5aed5f8-af97-444b-b204-77502ef61706 RC {ECO:0000313|EMBL:VVH50579.1}; RA Ansorge, R.; RL Submitted (SEP-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 --------------------------------------------------------------------------- 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; CABVGK010000029; VVH50579.1; -; 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: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; 4. 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, ECO:0000313|EMBL:VVH50579.1}; 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}; 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:VVH50579.1}; 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:VVH50579.1}. FT DOMAIN 6..125 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 9..12 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 78..79 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 100..102 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..452 FT /note="N-acetyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 383..384 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT ACT_SITE 360 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 102 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 23 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 73 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 137 FT /note="UDP-GlcNAc; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 151 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 166 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 330 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 348 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 363 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 374 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 377 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 402 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 420 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 437 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" SQ SEQUENCE 452 AA; 48382 MW; 3C0A92583EB61564 CRC64; MNNINAIILA AGKGTRMNST KPKVLQVLSD KTLLEHVLMQ AQALCSQVFV VVGFGSEQVC QALDDDSINW VEQSEQLGTG HAVQQATPYI NDDSISLVLY GDVPLIRQST LKDLITQTQK SGVALLSVML DNPAGYGRII RKDNQIQAIV EQKDANTEQL MICEVNTGIM VLDSGLLKAY LGNLNANNVQ GEFYLTDIIA MAVKDGKTIA SVIAENDSEV AGVNDKVQLA ELERVFQKNQ ANQFMQQGLT LKDPARFDCR GTLNFGQDCE VDVNVVVEGN VSLGDNTTIA PNCIIKNAKI GTNVVILPNS VIEDAIIGDG ASIGPFARIR PEAHIGESAK IGNFVEVKKS TIGKGSKISH LSYVGDTIMG EDVNIGAGVI TCNYDGVNKH QTTIEDGVFV GSDTQFIAPV TIGKNATIGA GSTIAKDVPG GKLSLSRTKQ AVLKNWKKPI KK //