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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)]

 A0A172SR74_CAMHY        Unreviewed;       436 AA.
A0A172SR74;
07-SEP-2016, integrated into UniProtKB/TrEMBL.
07-SEP-2016, sequence version 1.
16-JAN-2019, entry version 18.
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:ANE32692.1};
ORFNames=CHH_1045 {ECO:0000313|EMBL:ANE32692.1};
Campylobacter hyointestinalis subsp. hyointestinalis LMG 9260.
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=1031746 {ECO:0000313|EMBL:ANE32692.1, ECO:0000313|Proteomes:UP000076954};
[1] {ECO:0000313|EMBL:ANE32692.1, ECO:0000313|Proteomes:UP000076954}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LMG 9260 {ECO:0000313|EMBL:ANE32692.1,
ECO:0000313|Proteomes:UP000076954};
Miller W., Yee E.;
"Complete genome sequences of Campylobacter hyointestinalis subsp.
hyointestinalis strain LMG9260 and Campylobacter hyointestinalis
subsp. lawsonii strain RM15993.";
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
-!- 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}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01631}.
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EMBL; CP015575; ANE32692.1; -; Genomic_DNA.
RefSeq; WP_034961068.1; NZ_CP015575.1.
EnsemblBacteria; ANE32692; ANE32692; CHH_1045.
GeneID; 32076146; -.
KEGG; chyo:CHH_1045; -.
PATRIC; fig|1031746.3.peg.1051; -.
KO; K04042; -.
OrthoDB; 1381953at2; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000076954; 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; IPR025877; MobA-like_NTP_Trfase.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 1.
Pfam; PF12804; NTP_transf_3; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01173; glmU; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083661, ECO:0000313|EMBL:ANE32692.1};
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:UP000076954};
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, ECO:0000313|EMBL:ANE32692.1};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01631,
ECO:0000256|SAAS:SAAS00083721};
Reference proteome {ECO:0000313|Proteomes:UP000076954};
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,
ECO:0000313|EMBL:ANE32692.1}.
DOMAIN 7 122 NTP_transf_3. {ECO:0000259|Pfam:PF12804}.
REGION 1 226 Pyrophosphorylase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 9 12 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 82 83 UDP-GlcNAc binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 227 247 Linker. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 248 436 N-acetyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01631}.
REGION 362 363 Acetyl-CoA binding. {ECO:0000256|HAMAP-
Rule:MF_01631}.
ACT_SITE 339 339 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 105 105 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
METAL 224 224 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 23 23 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 75 75 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 138 138 UDP-GlcNAc; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 152 152 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 167 167 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 224 224 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 311 311 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 328 328 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 342 342 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 353 353 UDP-GlcNAc. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 381 381 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
BINDING 399 399 Acetyl-CoA; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01631}.
BINDING 416 416 Acetyl-CoA. {ECO:0000256|HAMAP-
Rule:MF_01631}.
SEQUENCE 436 AA; 47799 MW; 5879508771AFCC4C CRC64;
MNDISIIILA AGNGTRMKSS KSKVLHELCG EPMITHILKK SYEITSDVRV VLSYQFEEVK
SVVLAEFENT KICKQDTVNF PGTAGALRAA INDLNSKKTL IICGDMPLVQ VNELKALCEN
SSDVTLSTFK AIDPNGYGRV ITKDKKVVKI VEQKDANENE IKVDLCNAGA YCFDTNLLKD
LIPLIKNNNA SKEFYLTDAI ELAINRGFSV SFSLVSEANF MGINDKFALS LAEEIMQNSI
KEKLMKNGVI MHLPKTIFID SRAKFEGECI IEPNVMIIGN SVIKNSVIKS GSVIEYSQVD
SSDVGPMAHL RPNSKIKKTH IGNFVELKNA NLDTVKAGHL SYLGDCDISS GTNIGCGTIT
CNYDGKKKYK TIIGKNVFIG SDTQLVAPVS IADDTLVAAG STVTKDSNKG DLIITRNAQI
NKPMYFYKFF GKNDEK


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Kits Elisa; taq POLYMERASE

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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 :
[23485416] Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases.
[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.
[21594607] Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU.
[21370307] Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli.
[19804974] Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12.
[18573680] Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase.
[11329257] Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
[11173485] Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
[11118459] Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
[11084021] Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth.