GLMU_VIBC1
ID GLMU_VIBC1 Reviewed; 453 AA.
AC A7N0Z7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631};
GN OrderedLocusNames=VIBHAR_00419;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01631}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000255|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; CP000789; ABU69434.1; -; Genomic_DNA.
DR RefSeq; WP_012126653.1; NC_022269.1.
DR AlphaFoldDB; A7N0Z7; -.
DR SMR; A7N0Z7; -.
DR PRIDE; A7N0Z7; -.
DR EnsemblBacteria; ABU69434; ABU69434; VIBHAR_00419.
DR KEGG; vha:VIBHAR_00419; -.
DR PATRIC; fig|338187.25.peg.2171; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 1381953at2; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000008152; Chromosome I.
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; 3.
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; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW Peptidoglycan synthesis; Repeat; Transferase.
FT CHAIN 1..453
FT /note="Bifunctional protein GlmU"
FT /id="PRO_1000069738"
FT REGION 1..226
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 227..247
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 248..453
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 360
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 8..11
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 22
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 73
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 78..79
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 100..102
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 137
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 151
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 166
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 224
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 330
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 348
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 363
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 374
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 377
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 383..384
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 402
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 420
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 437
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ SEQUENCE 453 AA; 48572 MW; D9F14CD8D4CB7A10 CRC64;
MKFSAVILAA GKGTRMYSNM PKVLHTLAGK PMAKHVIDTC TGLGAQNIHL VYGHGGDQMQ
QTLAEEPVNW VLQAEQLGTG HAVDQASPKF EDDEKVLVLY GDVPLISAET IENLLDAQPT
GGIALLTVML DNPMGYGRII RKNGPVVAIV EQKEATEEQK LIKECNTGVL VATGGDLKRW
LAGLNNENAQ GEYYLTDVIA AAHDEGRAVE AVHPVNAIEV EGVNDRAQLA RLERAFQSMQ
AQKLLEQGVM LRDPARFDLR GELQCGMDCE IDANVVIEGK VSLGDNVVIG AGCVLKDCEI
DDNTVVRPYS VIEGATVGEE CTVGPFTRLR PGAEMRNDSH VGNFVEVKNA CIGEGSKANH
LTYLGDAEIG QRTNIGAGTI TCNYDGANKF KTVIGNDVFV GSDSQLVAPV TIADGATIGA
GTTLTKDVAE GELVITRVKE RKITGWQRPV KQK
