GLMU_ACTPJ
ID GLMU_ACTPJ Reviewed; 454 AA.
AC B0BUE6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=APJL_0581;
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03;
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY69151.1; -; Genomic_DNA.
DR RefSeq; WP_012262868.1; NC_010278.1.
DR AlphaFoldDB; B0BUE6; -.
DR SMR; B0BUE6; -.
DR EnsemblBacteria; ABY69151; ABY69151; APJL_0581.
DR KEGG; apj:APJL_0581; -.
DR HOGENOM; CLU_029499_15_2_6; -.
DR OMA; TAIVEHK; -.
DR OrthoDB; 1381953at2; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000008547; 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; Repeat; Transferase.
FT CHAIN 1..454
FT /note="Bifunctional protein GlmU"
FT /id="PRO_1000186387"
FT REGION 1..227
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 228..248
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT REGION 249..454
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 9..12
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 23
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 74
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 79..80
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 101..103
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 138
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 152
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 167
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 225
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 331
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 349
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 364
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 375
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 378
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 384..385
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 403
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 421
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 438
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
SQ SEQUENCE 454 AA; 48987 MW; 01665FA7DBFAB5DC CRC64;
MTQLSVVILA AGKGTRMYSD LPKVLHTVAG KPMVQHVIDT AKQIDAKQIH LIYGHGGELL
QQRLSSEPVN WVLQAEQLGT GHAMQQAAPF FADDENILML YGDAPLITKE TLERLIAAKP
ANGIALLTVE LENPNGYGRI IRENGSVVAI VEQKDANAEQ LKICEVNTGV MVASGASFKK
WLANLNNNNA QGEYYITDVI AMANQDGYKV QAVQASEFME VEGANNRLQL AALERFYQKT
QAEKLLLAGV RLIDPARFDI RGSLTHGKDV EIDVNVIIEG EVKLGNRVRI CAGCVLKNCE
IGDDVEIKPY SVIEDAVVGK AAQIGPFSRL RPGANLAEET HVGNFVEIKN AQIGKGSKVN
HLTYVGDAEV GSNCNIGAGV ITCNYDGANK FKTIIGNNVF VGSDSQLVAP VTIADGATIG
AGATVTKDVA ENELVISRVP QRHIQGWQRP TKKK
