ID A0A0H3H5X9_KLEOK Unreviewed; 456 AA. AC A0A0H3H5X9; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 26-FEB-2020, entry version 32. 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:AEX03067.1}; GN OrderedLocusNames=KOX_06685 {ECO:0000313|EMBL:AEX03067.1}; OS Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / OS NRRL B-199 / KCTC 1686). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1006551 {ECO:0000313|EMBL:AEX03067.1, ECO:0000313|Proteomes:UP000007843}; RN [1] {ECO:0000313|Proteomes:UP000007843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / RC KCTC 1686 {ECO:0000313|Proteomes:UP000007843}; RA Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.; RT "Complete genome sequence of Klebsiella oxytoca strain KCTC 1686."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEX03067.1, ECO:0000313|Proteomes:UP000007843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / RC KCTC 1686 {ECO:0000313|Proteomes:UP000007843}; RX PubMed=22493189; DOI=10.1128/JB.00026-12; RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J., RA Yang K.S.; RT "Complete Genome Sequence of Klebsiella oxytoca KCTC 1686, Used in RT Production of 2,3-Butanediol."; RL J. Bacteriol. 194:2371-2372(2012). 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, 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; 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 ECO:0000256|SAAS:SAAS01124206}; 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 ECO:0000256|SAAS:SAAS01124218}; 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, ECO:0000256|SAAS:SAAS00083707}. 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, 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. {ECO:0000256|HAMAP- CC 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; CP003218; AEX03067.1; -; Genomic_DNA. DR RefSeq; WP_014227347.1; NC_016612.1. DR EnsemblBacteria; AEX03067; AEX03067; KOX_06685. DR KEGG; kox:KOX_06685; -. DR PATRIC; fig|1006551.4.peg.1339; -. DR HOGENOM; CLU_029499_15_2_6; -. DR KO; K04042; -. DR OMA; QNAQKEY; -. DR BioCyc; KOXY1006551:G1H2C-1375-MONOMER; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000007843; Chromosome. 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; 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, ECO:0000313|EMBL:AEX03067.1}; 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, ECO:0000256|SAAS:SAAS00458650}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01631, 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 Repeat {ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00458660}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458747, ECO:0000313|EMBL:AEX03067.1}. FT DOMAIN 8..123 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 81..82 FT /note="UDP-GlcNAc binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 103..105 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..456 FT /note="N-acetyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT REGION 386..387 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT ACT_SITE 363 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT METAL 105 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 76 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 140 FT /note="UDP-GlcNAc; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 154 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 169 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 333 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 351 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 366 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 377 FT /note="UDP-GlcNAc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 380 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 405 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 423 FT /note="Acetyl-CoA; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" FT BINDING 440 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01631" SQ SEQUENCE 456 AA; 49359 MW; 4DB13E6473D38D34 CRC64; MSNSPMSVVI LAAGKGTRMY SDLPKVLHSL AGKPMVQHVI DAAKELGASA VHLVYGHGGD LLRQTLHEDN LNWVLQAEQL GTGHAMQQAA PFFSDDEDIL MLYGDVPLIS VETLKRLREA KPQGGIGLLT VKLDDPTGYG RITRDNGAVT GIVEHKDASD EQRRIQEINT GILVANGADL KRWLAKLTNN NVQGEYYITD IIAMAYEEGR EIAAVHPQRL SEVEGVNNRL QLSRLERVWQ SEKAEELLLA GVMLRDPARF DLRGVLKHGR DVEIDTNVIF EGDVVLGDRV KIGTGCVIKN STIGDDCEIS PYTVVEDAHL EAACTIGPFA RLRPGAELLE GAHVGNFVEI KKARLGKGTK AGHLSYLGDA EIGDNVNIGA GTITCNYDGA NKHKTVIGDD VFVGSDSQLV APVTVGKGVT IAAGTTVTRN VADNELVLSR VPQVHKQGWQ RPVKKK //