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Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]

 C8UJC0_ECO1A            Unreviewed;       456 AA.
C8UJC0;
03-NOV-2009, integrated into UniProtKB/TrEMBL.
03-NOV-2009, sequence version 1.
16-JAN-2019, entry version 68.
RecName: Full=Bifunctional protein GlmU {ECO:0000256|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
EC=2.3.1.157 {ECO:0000256|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01631};
EC=2.7.7.23 {ECO:0000256|HAMAP-Rule:MF_01631};
AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000256|HAMAP-Rule:MF_01631};
Name=glmU {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000313|EMBL:BAI38314.1};
OrderedLocusNames=ECO111_4563 {ECO:0000313|EMBL:BAI38314.1};
Escherichia coli O111:H- (strain 11128 / EHEC).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=585396 {ECO:0000313|EMBL:BAI38314.1, ECO:0000313|Proteomes:UP000001614};
[1] {ECO:0000313|EMBL:BAI38314.1, ECO:0000313|Proteomes:UP000001614}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=11128 / EHEC {ECO:0000313|Proteomes:UP000001614};
PubMed=19815525; DOI=10.1073/pnas.0903585106;
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
Hayashi T.;
"Comparative genomics reveal the mechanism of the parallel evolution
of O157 and non-O157 enterohemorrhagic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
-!- FUNCTION: Catalyzes the last two sequential reactions in the de
novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-
GlcNAc). The C-terminal domain catalyzes the transfer of acetyl
group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P)
to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is
converted into UDP-GlcNAc by the transfer of uridine 5-
monophosphate (from uridine 5-triphosphate), a reaction catalyzed
by the N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083685}.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
diphosphate + UDP-N-acetyl-alpha-D-glucosamine;
Xref=Rhea:RHEA:13509, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
ChEBI:CHEBI:46398, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776;
EC=2.7.7.23; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS01124206};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+)
+ N-acetyl-alpha-D-glucosamine 1-phosphate;
Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516;
EC=2.3.1.157; Evidence={ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS01124218};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01631};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01631};
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083707}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate
from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381596}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00381463}.
-!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00569615}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00381517}.
-!- SIMILARITY: In the C-terminal section; belongs to the transferase
hexapeptide repeat family. {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00569628}.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylglucosamine-1-phosphate uridyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_01631, ECO:0000256|SAAS:SAAS00569629}.
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EMBL; AP010960; BAI38314.1; -; Genomic_DNA.
RefSeq; WP_000933736.1; NC_013364.1.
ProteinModelPortal; C8UJC0; -.
SMR; C8UJC0; -.
EnsemblBacteria; BAI38314; BAI38314; ECO111_4563.
KEGG; eoi:ECO111_4563; -.
HOGENOM; HOG000283476; -.
KO; K04042; -.
OMA; IEPQTHL; -.
BioCyc; ECOL585396:ECO111_RS23865-MONOMER; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000001614; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-UniRule.
GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd03353; LbH_GlmU_C; 1.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_01631; GlmU; 1.
InterPro; IPR005882; Bifunctional_GlmU.
InterPro; IPR038009; GlmU_C_LbH.
InterPro; IPR001451; Hexapep.
InterPro; IPR018357; Hexapep_transf_CS.
InterPro; IPR025877; MobA-like_NTP_Trfase.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 3.
Pfam; PF12804; NTP_transf_3; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01173; glmU; 1.
PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083661};
Cell shape {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083688};
Complete proteome {ECO:0000313|Proteomes:UP000001614};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083649};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083580};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083557};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00458631};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083639};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Repeat {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083725};
Transferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083639, ECO:0000256|SAAS:SAAS00083661}.
DOMAIN 8 123 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 229 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 11 14 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 81 82 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 103 105 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 230 250 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 251 456 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 386 387 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 363 363 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 105 105 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 227 227 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 25 25 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 76 76 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 140 140 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 154 154 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 169 169 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 227 227 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 333 333 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 351 351 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 366 366 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 377 377 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 380 380 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 405 405 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 423 423 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 440 440 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
SEQUENCE 456 AA; 49190 MW; 2F3C5C84F673C8A3 CRC64;
MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD
LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA
KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM
KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ
SEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN
SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK
AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT
IAAGTTVTRN VGENALAISR VPQTQKEGWR RPVKKK


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G5409 Putative N-acetylglucosamine-6-phosphate deacetylase (AMDHD2), Human, ELISA Kit 96T
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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1657: Glycerolipid metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1028: Pentose Phosphate Pathway
WP1147: Pentose Phosphate Pathway
WP122: Pentose Phosphate Pathway
WP1231: Pentose Phosphate Pathway
WP134: Pentose Phosphate Pathway
WP1658: Glycerophospholipid metabolism
WP1664: Inositol phosphate metabolism
WP1665: Limonene and pinene degradation
WP1684: Pentose phosphate pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1690: Propanoate metabolism
WP1713: Two-component system
WP1714: Tyrosine metabolism
WP2185: Purine metabolism
WP220: Ribose and Deoxyribose Phosphate Metabolism
WP2212: Methylerythritol phosphate pathway
WP228: Deoxyribose phosphate metabolism
WP253: Glycolysis
WP260: Glucose-1-phosphate metabolism
WP282: Pentose Phosphate Pathway
WP312: Pentose Phosphate Pathway

Related Genes :
[glmU yieA b3730 JW3708] Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
[glmU SP_0988] Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
[glmU Rv1018c] Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
[glmU MSMEG_5426 MSMEI_5277] Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
[glmU OR1_01412] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPP23_1065] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPH23_1130] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU MJ1101] Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]
[glmU HPHPP1_0927] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPP2_0781] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU OR37_01460] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU OR221_2794] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPP3_0872] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPH3_0875] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPA4_0897] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPP16_0834] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPA8_0591] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU OUG_0451] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPA26_0689] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPCPY1124_0840] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPP11_1021] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPNQ4099_0928] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPNQ4200_0752] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU OUS_1094] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPH45_0735] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU OUM_0835] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPNQ4076_0759] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPNQ4228_1149] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPH27_1328] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU HPHPP30_1305] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]

Bibliography :
[25544688] Identification and optimization of Escherichia coli GlmU inhibitors: an in silico approach with validation thereof.
[23099094] Inhibitors of the acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 2: Optimization of physical properties leading to antibacterial aryl sulfonamides.
[22969087] Substrate-bound crystal structures reveal features unique to Mycobacterium tuberculosis N-acetyl-glucosamine 1-phosphate uridyltransferase and a catalytic mechanism for acetyl transfer.
[22721802] An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.
[21984832] In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae.
[21594607] Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU.
[19237750] Structure and function of GlmU from Mycobacterium tuberculosis.
[18573680] Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase.
[17473010] Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
[11329257] Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
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