Rv1018c - UDP-N-acetylglucosamine pyrophosphorylase glmU
Protein Domains

Gene Information
LocusRv1018c
SymbolglmU
Gene NameUDP-N-acetylglucosamine pyrophosphorylase glmU
Location1136573 - 1138060 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:1488 bp
Protein:496 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
Search Google Scholar
Orthologs
Orthogroup Number405
Related GenesAcel_1947 BL0964 CE1016 cg1076 DIP0904 jk1492 MAP0984c MAV_1157 Mkms_4334 ML0249 Mmcs_4248 MSMEG_5426 MT1046 MUL_4637 Mvan_4782 nfa48780 PPA0530 SAV3561
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv1018c
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionPhysicalInteraction Rv0014cactiveashwinigbhat2012-10-05
Structural Analysis
A. Parikh, SK. Verma et al. PknB-Mediated Phosphorylation of a Novel Substrate, N-Acetylglucosamine-1-Phosphate Uridyltransferase, Modulates Its Acetyltransferase Activity. J. Mol. Biol. 2008
InteractionPhysicalInteraction Rv0014cactiveashwinigbhat2012-10-05
Structural Analysis
W. Zhang, VC. Jones et al. Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. Int. J. Biochem. Cell Biol. 2008
InteractionPhysicalInteraction Rv0014cactivepriti.priety2012-10-05
Structural Analysis
A. Parikh, SK. Verma et al. PknB-Mediated Phosphorylation of a Novel Substrate, N-Acetylglucosamine-1-Phosphate Uridyltransferase, Modulates Its Acetyltransferase Activity. J. Mol. Biol. 2008
InteractionPhysicalInteraction Rv0014cactivepriti.priety2012-10-05
Structural Analysis
W. Zhang, VC. Jones et al. Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. Int. J. Biochem. Cell Biol. 2008
InteractionRegulatedBy Rv0485activeyamir.moreno2012-10-05
E.coli orthology based inference. Orthologous pair regulator-target found in E.coli.
G. Balázsi, AP. Heath et al. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 2008
InteractionRegulatedBy Rv0485activeyamir.moreno2012-10-05
E.coli orthology based inference. Orthologous pair regulator-target found in E.coli.
authors,M. Madan Babu,SA. Teichmann,L. Aravind Evolutionary dynamics of prokaryotic transcriptional regulatory networks. J. Mol. Biol. 2006
NameBifunctional enzyme: N-acetylation of GlcNH2-1-P to form GlcNAc-1-P and GlcNAc-1-P uridylyltransferase that forms UDP-GlcNAcactivemjackson2012-10-05
UDP-GlcNAc synthesis
TermGO:0006048 UDP-N-acetylglucosamine biosynthetic process - NRactivemmcneil2012-03-05
N-acetylation of GlcNH2-1-P to form GlcNAc-1-P by the bifunctional enzyme GlmU; enzymatic evidence
W. Zhang, VC. Jones et al. Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. Int. J. Biochem. Cell Biol. 2008
TermGO:0006048 UDP-N-acetylglucosamine biosynthetic process - NRactivemmcneil2012-03-05
Conversion of glcNH2-6-P to glcNH2-1-P (unpublished data Michael McNeil; enzymatic evidence)
W. Zhang, VC. Jones et al. Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. Int. J. Biochem. Cell Biol. 2008