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GLMU_LACJO
ID   GLMU_LACJO              Reviewed;         461 AA.
AC   Q74LH7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
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}; OrderedLocusNames=LJ_0208;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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}.
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DR   EMBL; AE017198; AAS08190.1; -; Genomic_DNA.
DR   RefSeq; WP_004898713.1; NC_005362.1.
DR   AlphaFoldDB; Q74LH7; -.
DR   SMR; Q74LH7; -.
DR   STRING; 257314.LJ_0208; -.
DR   EnsemblBacteria; AAS08190; AAS08190; LJ_0208.
DR   KEGG; ljo:LJ_0208; -.
DR   eggNOG; COG1207; Bacteria.
DR   HOGENOM; CLU_029499_15_2_9; -.
DR   OMA; TAIVEHK; -.
DR   UniPathway; UPA00113; UER00532.
DR   UniPathway; UPA00113; UER00533.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000581; 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: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; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..461
FT                   /note="Bifunctional protein GlmU"
FT                   /id="PRO_0000233786"
FT   REGION          1..229
FT                   /note="Pyrophosphorylase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          230..250
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   REGION          251..461
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   ACT_SITE        362
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         72
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         77..78
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         139
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         154
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         169
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         227
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         332
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         350
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         365
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         376
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         385..386
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         422
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT   BINDING         439
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ   SEQUENCE   461 AA;  50198 MW;  275D8B961079D927 CRC64;
     MNKYVVILAA GKGTRMKSKL YKVLHKVCGK TMVEHVVEAA KGTNPDKIIT VVGNGAESVK
     DVLAGQSEFA FQEKQLGTGD AVLAANDLLE NLEGSTLVAT GDTPLFTAET FNNLFKKHEE
     SGNSATVLTA KAPNPFGYGR IIRDEDGNVL RIVEQKDGTP EELAVDEINT GVFCFDNKEL
     FKALKQVGND NAQGEYYLTD VLEIMRKAGH KVGAYEMPDF SESLGVNDRI ALAQATKIMQ
     RRINEEHMRN GVSFIDPDTA YIDSDVKIGN DTVIEGNVVI KGKTEIGSNC YITNSSRIID
     SKIGNNVTIT SSTLQEAQMD DNTDIGPNSH LRPKAVIRKG AHIGNFVEIK KAEIGENTKV
     GHLTYVGDAT LGKDINIGCG TIFSNYDGVK KFHTNVGDHS FIGAGATIIA PVNIADHAFV
     AADSTITKDV EKYDMAIARG RQTNKPDYWH KLPLAKDKEW E
 
 
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