ID A0A934TQ13_9BURK Unreviewed; 467 AA. AC A0A934TQ13; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 27-NOV-2024, entry version 8. 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:MBK6004846.1}; GN ORFNames=JJB11_01975 {ECO:0000313|EMBL:MBK6004846.1}; OS Ramlibacter ginsenosidimutans. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=502333 {ECO:0000313|EMBL:MBK6004846.1, ECO:0000313|Proteomes:UP000630528}; RN [1] {ECO:0000313|EMBL:MBK6004846.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 17527 {ECO:0000313|EMBL:MBK6004846.1}; RX PubMed=22450785; RA Wang L., An D.S., Kim S.G., Jin F.X., Kim S.C., Lee S.T., Im W.T.; RT "Ramlibacter ginsenosidimutans sp. nov., with ginsenoside-converting RT activity."; RL J. Microbiol. Biotechnol. 22:311-315(2012). RN [2] {ECO:0000313|EMBL:MBK6004846.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 17527 {ECO:0000313|EMBL:MBK6004846.1}; RA Kang M.; RL Submitted (JAN-2021) 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=N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N- CC acetyl-alpha-D-glucosamine + diphosphate; 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|ARBA:ARBA00001851, ECO:0000256|HAMAP- CC Rule:MF_01631}; CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha- CC D-glucosamine 1-phosphate + CoA + H(+); 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|ARBA:ARBA00000731, ECO:0000256|HAMAP- CC 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:MBK6004846.1}. 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; JAEPWM010000001; MBK6004846.1; -; Genomic_DNA. DR Proteomes; UP000630528; 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-UniRule. 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:InterPro. DR CDD; cd02540; GT2_GlmU_N_bac; 1. DR CDD; cd03353; LbH_GlmU_C; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR050065; GlmU-like. 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 NCBIfam; TIGR01173; glmU; 1. DR PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1. DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 1. DR Pfam; PF00132; Hexapep; 2. DR Pfam; PF14602; Hexapep_2; 1. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_01631}; Reference proteome {ECO:0000313|Proteomes:UP000630528}; 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}. FT DOMAIN 6..135 FT /note="MobA-like NTP transferase" FT /evidence="ECO:0000259|Pfam:PF12804" FT REGION 1..234 FT /note="Pyrophosphorylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 235..255 FT /note="Linker" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 256..467 FT /note="N-acetyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT ACT_SITE 372 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 23 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 81 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 86..87 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 110 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 145 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 159 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 232 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 342 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 360 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 375 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 386 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 389 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 395..396 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 414 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 432 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 449 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" SQ SEQUENCE 467 AA; 49473 MW; 942F1F03EA59EC07 CRC64; MTAVDVVVMA AGKGTRMKSR TAKVLHRLGG RPLIAHVMDT AHALAARRTI VITGHGAEDV EGWLRSAAAA QGRPSPDFVR QEPQLGTGHA VQQAVPVLPD DGIALILNGD VPLIRPETLQ ALVDKCGGER LALLTVEMAD PTGYGRILRR GDAVQAIVEH KDASAAQRGI REVYTGFMAV PERKLKTWLA RLSNDNAQRE YYLTDIVQFA VADGCEVVAS PAAEQVEVDG VNSPLQLAAL ERAFQSRQAN ALMEQGVRLA DPARFDLRGR LSCGQDVEID VNCVFQGEVS LGDNVRIGPN CVISNAKIAA NVVLQAYTHI EGEEAGVEIG EGALIGPFAR LRPGAQLGPE VHIGNFVEVK NSTLARGAKA NHLAYLGDTT VGERVNYGAG SITANYDGAN KNRTVIEADV HVGSNCVLVA PVTVAKGGTI GAGSVVNKNT EPGALTVARA KQVSITNWQR PKKAAKK //