ID A0A433CUZ6_ACISP Unreviewed; 454 AA. AC A0A433CUZ6; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-JUL-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:RUP42382.1}; GN ORFNames=EKK63_01605 {ECO:0000313|EMBL:RUP42382.1}; OS Acinetobacter sp. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=472 {ECO:0000313|EMBL:RUP42382.1, ECO:0000313|Proteomes:UP000281910}; RN [1] {ECO:0000313|EMBL:RUP42382.1, ECO:0000313|Proteomes:UP000281910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWTP1-36 {ECO:0000313|EMBL:RUP42382.1}; RA Kantor R.S., Miller S.E., Nelson K.L.; RT "The water microbiome through an advanced treatment facility for RT direct potable reuse."; RL Submitted (NOV-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}. 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:RUP42382.1}. 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; RXKH01000015; RUP42382.1; -; Genomic_DNA. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00973; -. DR Proteomes; UP000281910; 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-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; 2. DR Pfam; PF14602; Hexapep_2; 1. 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|HAMAP-Rule:MF_01631, KW ECO:0000256|SAAS:SAAS00458646, ECO:0000313|EMBL:RUP42382.1}; 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}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000281910}; 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:RUP42382.1}; 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:RUP42382.1}. FT DOMAIN 5 127 NTP_transf_3. {ECO:0000259|Pfam:PF12804}. FT REGION 1 226 Pyrophosphorylase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 8 11 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 78 79 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 100 102 UDP-GlcNAc binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 227 247 Linker. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT REGION 248 454 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT REGION 383 384 Acetyl-CoA binding. {ECO:0000256|HAMAP- FT Rule:MF_01631}. FT COILED 227 247 {ECO:0000256|SAM:Coils}. FT ACT_SITE 360 360 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 102 102 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT METAL 224 224 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 22 22 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 73 73 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 137 137 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 151 151 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 166 166 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 224 224 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 330 330 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 348 348 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 363 363 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 374 374 UDP-GlcNAc. {ECO:0000256|HAMAP-Rule: FT MF_01631}. FT BINDING 377 377 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 420 420 Acetyl-CoA; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01631}. FT BINDING 437 437 Acetyl-CoA. {ECO:0000256|HAMAP-Rule: FT MF_01631}. SQ SEQUENCE 454 AA; 49237 MW; 662C26F318032E1F CRC64; MSTTVIILAA GKGTRMRSQL PKVLQPLAGR PLLGHVIQTA KKLHAQNIIT IYGHGGDLVK QSFAAEQIEW VEQAEQLGTG HAVQMTLPVL PQDGISLILY GDVPLVRQST LEQLLEASSH SGIGMITLNV ENPTGYGRIV RQAGKIQAIV EHKDANDEQR QIQEINTGIY CVSNAQLHQW LPKLSNNNVQ GEYYLTDIVA MAVADGLEIA SIQPELAFEV EGVNDRLQLA TLERQFQQQQ AKELMLQGVH LIDPNRFDLR GSVKCGQDVQ IDVNVIIEGD CELGDNVQLG AGCILKNTRI AAGTKVQAYS VFENAIVGEN TQIGPFARLR PGANLADDVH IGNFVEVKNT NMGQGSKANH FTYLGDADIG ANCNIGAGTI TCNYDGANKH RTIIEDNVFI GTNNSLVAPI KIGQGATTGA GSTLTRNVAE HSLAVERSKQ FEKANYQRPQ KLKK //