GLMU_BACCL
ID GLMU_BACCL Reviewed; 116 AA.
AC P42817;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Bifunctional protein GlmU;
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase;
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase;
DE EC=2.3.1.157;
DE Flags: Fragment;
GN Name=glmU; Synonyms=gcaD;
OS Bacillus caldolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX PubMed=8918235; DOI=10.1016/0378-1119(96)00222-3;
RA Krath B.N., Hove-Jensen B.;
RT "Bacillus caldolyticus prs gene encoding phosphoribosyl-diphosphate
RT synthase.";
RL Gene 176:73-79(1996).
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 (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
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 -!- 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 -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000305}.
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DR EMBL; X83708; CAA58681.1; -; Genomic_DNA.
DR PIR; PC4228; PC4228.
DR AlphaFoldDB; P42817; -.
DR SMR; P42817; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
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-KW.
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 InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 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..116
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000068705"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 116 AA; 12106 MW; D27706B9B8F7BB62 CRC64;
IGNFVEVKKS TFGKGSKAPH LSYIGDAEVG ADVNLGCGSI TVNYDGVNKH MTKIENGAFI
GCNVNLIAPV TVGQGAYVAA GSTITNDVPG RALAIARARQ VNKENYVDRL PGKKKS
