glmU



Type
protein_coding
Name
glmU
Locus Name

Rv1018c

Product

Probable UDP-N-acetylglucosamine pyrophosphorylase GlmU

Functional Category

Cell wall and cell processes

Location
1136573..1138060 (- strand)
Gene Length
1487 bp
Nucleotides
ATGACGTTTCCTGGTGACACCGCGGTCCTGGTCCTAGCGGCCGGGCCCGGGACCCGGATGCGTTCGGACACCCCCAAGGTGCTGCACACACTCGCCGGTCGCAGCATGCTGTCGCATGTACTGCATGCGATCGCCAAGCTGGCGCCGCAGCGTCTAATCGTGGTGCTGGGACACGATCACCAGCGCATCGCGCCGCTAGTCGGTGAACTCGCCGACACCCTAGGCCGAACGATCGACGTCGCCCTGCAGGATCGACCGCTAGGGACCGGGCATGCGGTACTCTGCGGGCTGTCCGCGCTGCCCGATGACTACGCCGGCAACGTCGTGGTCACCTCGGGAGATACCCCGCTGCTGGACGCCGACACGCTGGCCGACTTGATCGCCACCCACCGCGCGGTGTCGGCTGCGGTGACGGTGCTGACCACGACGCTGGATGATCCCTTCGGCTACGGCCGCATCCTGCGCACCCAGGATCACGAAGTCATGGCGATCGTGGAGCAAACCGACGCGACACCATCGCAGCGGGAAATCCGCGAAGTCAACGCCGGCGTCTACGCCTTCGACATCGCCGCGCTGCGGTCCGCACTGAGCCGGCTGAGCTCCAACAACGCCCAACAGGAGCTCTACCTCACCGACGTCATCGCCATCTTGCGCTCCGACGGCCAGACCGTACATGCCAGCCACGTCGACGACAGCGCGTTGGTGGCCGGCGTCAACAATCGCGTCCAGCTGGCCGAGCTGGCCTCCGAACTCAACCGGCGGGTGGTGGCCGCTCACCAGCTGGCCGGCGTCACCGTCGTCGACCCGGCTACCACCTGGATCGACGTCGACGTCACCATCGGCCGCGACACCGTCATTCACCCGGGTACCCAGTTGCTGGGCCGCACCCAGATCGGCGGTCGCTGTGTCGTCGGTCCCGACACCACCCTGACCGACGTCGCCGTCGGCGACGGTGCCTCGGTGGTGCGCACCCACGGTTCGTCGTCGTCGATTGGGGATGGCGCCGCGGTCGGGCCCTTCACCTACCTGCGGCCCGGAACCGCGTTGGGCGCCGACGGCAAGCTGGGCGCGTTCGTCGAGGTCAAGAACTCCACCATCGGCACCGGCACCAAGGTGCCGCACCTGACCTACGTCGGCGACGCCGACATCGGCGAGTACAGCAACATCGGCGCCTCCAGCGTGTTCGTCAACTACGACGGTACGTCCAAACGGCGCACCACCGTCGGTTCGCACGTACGGACCGGGTCCGACACCATGTTCGTGGCCCCAGTAACCATCGGCGACGGCGCGTATACCGGGGCCGGCACAGTGGTGCGGGAGGATGTCCCGCCGGGGGCGCTGGCAGTGTCGGCGGGTCCGCAACGCAACATCGAGAACTGGGTGCAGCGCAAACGCCCCGGCAGCCCAGCGGCTCAGGCCTCAAAAAGAGCCTCAGAAATGGCCTGCCAACAGCCCACACAACCACCCGACGCTGATCAGACACCGTG
Drug Resistance

Check for drug resistance association at TBDREAMDB

Mutations

Check for mutants available at TARGET


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:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:19237750}.
Family

N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family

GO
InterPro

UniProt
P9WMN3
GenBank
Rv1018c
EnsemblBacteria
Rv1018c
Mycobrowser
Rv1018c


2QKX
Summary
Name
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)]
Family
N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family
Protein Sequence
MTFPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLGRTIDVALQDRPLGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGSPAAQASKRASEMACQQPTQPPDADQTP
Mass
51,584 Da
Length
495 Aa

Rv1018c doesn't seem to be a targeted by any drug.



Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases.
J Mol Biol. 2013 May 27;425(10):1745-59. doi: 10.1016/j.jmb.2013.02.019. Epub 2013 Feb 26.
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.
J Mol Biol. 2009 Feb 20;386(2):451-64. doi: 10.1016/j.jmb.2008.12.031. Epub 2008 Dec 24.
Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt 5):435-9. doi: 10.1107/S1744309109010252. Epub 2009 Apr 24.
Structure and function of GlmU from Mycobacterium tuberculosis.
Acta Crystallogr D Biol Crystallogr. 2009 Mar;65(Pt 3):275-83. doi: 10.1107/S0907444909001036. Epub 2009 Feb 20.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis [corrected] .
PLoS One. 2010 Jan 6;5(1):e8589. doi: 10.1371/journal.pone.0008589.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.