Gene - combatTB X

glnA2

Type: protein_coding
Name: glnA2
Locus Name: Rv2222c
Product: Probable glutamine synthetase GlnA2 (glutamine synthase) (GS-II)
Functional Category: Intermediary metabolism and respiration
Location: 2492402..2493742 (- strand)
Gene Length: 1340 bp
Nucleotides: ATGGACCGACAGAAGGAATTCGTTCTTCGTACCCTGGAAGAACGCGACATCCGCTTCGTCCGGCTGTGGTTCACAGACGTGCTCGGTTTCCTCAAGTCGGTCGCCATCGCCCCAGCCGAACTCGAGGGCGCCTTCGAGGAAGGCATCGGCTTCGACGGATCCTCGATCGAGGGCTTTGCGCGGGTCTCGGAATCCGATACGGTGGCGCACCCGGACCCGTCGACCTTCCAGGTGCTGCCCTGGGCCACCAGTTCCGGCCACCACCACTCAGCGCGGATGTTTTGCGACATCACCATGCCGGACGGCTCGCCGTCGTGGGCGGACCCGCGGCACGTGTTGCGGCGGCAGCTGACGAAGGCCGGCGAACTCGGCTTCTCCTGCTACGTGCATCCCGAAATCGAGTTCTTCCTGCTCAAGCCCGGACCCGAGGACGGGTCGGTGCCCGTCCCGGTCGACAACGCCGGCTATTTCGACCAAGCGGTGCACGACTCCGCCTTGAACTTTCGCCGCCACGCGATCGATGCCCTGGAATTCATGGGCATCTCGGTGGAGTTCAGCCATCACGAAGGCGCACCCGGCCAGCAGGAGATCGACCTGCGGTTTGCCGACGCTCTGTCGATGGCTGACAACGTGATGACCTTCCGCTACGTCATCAAAGAAGTCGCGCTGGAAGAGGGCGCCCGGGCGTCGTTCATGCCCAAGCCATTCGGCCAGCACCCGGGCTCGGCGATGCACACCCACATGAGCCTGTTCGAGGGTGATGTCAACGCGTTCCACAGCGCTGATGATCCGCTGCAGCTGTCGGAAGTGGGTAAATCGTTCATCGCCGGGATCCTGGAGCACGCTTGCGAGATCAGCGCGGTCACAAATCAGTGGGTCAACTCTTACAAGCGGCTGGTGCAGGGCGGCGAAGCGCCCACGGCCGCGTCGTGGGGGGCCGCCAACCGATCCGCCCTAGTGCGGGTGCCGATGTACACGCCGCACAAGACCTCGTCGCGGCGGGTCGAAGTACGCAGCCCTGATTCGGCGTGCAATCCCTATCTGACATTCGCCGTGCTGCTGGCCGCGGGATTGCGGGGTGTAGAGAAGGGTTACGTGCTGGGCCCGCAGGCCGAGGACAACGTATGGGACCTCACACCCGAGGAACGCCGAGCGATGGGGTACCGAGAATTGCCGTCCAGTTTGGATAGTGCGCTGCGCGCCATGGAGGCCTCCGAACTCGTCGCGGAGGCCTTGGGGGAGCACGTTTTTGACTTTTTCTTGCGCAACAAGCGCACGGAGTGGGCGAACTACCGCAGCCACGTCACGCCATACGAGCTGCGCACCTACCTGTCGCTGTA
Drug Resistance: Check for drug resistance association at TBDREAMDB
Mutations: Check for mutants available at TARGET

Function

Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes. {ECO:0000250|UniProtKB:P12425}.

Family

Glutamine synthetase family

GO

glutamate-ammonia ligase activity GO:0004356 molecular_function
glutamine biosynthetic process GO:0006542 biological_process
polyamine catabolic process GO:0006598 biological_process
transcription factor binding GO:0008134 molecular_function
cytoplasm GO:0005737 cellular_component
plasma membrane GO:0005886 cellular_component
ATP binding GO:0005524 molecular_function
D-glutaminase activity GO:0050001 molecular_function
metal ion binding GO:0046872 molecular_function

InterPro

UniProt: P9WN37
GenBank: Rv2222c
EnsemblBacteria: Rv2222c
Mycobrowser: Rv2222c

Summary

Name: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I alpha) (GSI alpha)
Family: Glutamine synthetase family
Protein Sequence: MDRQKEFVLRTLEERDIRFVRLWFTDVLGFLKSVAIAPAELEGAFEEGIGFDGSSIEGFARVSESDTVAHPDPSTFQVLPWATSSGHHHSARMFCDITMPDGSPSWADPRHVLRRQLTKAGELGFSCYVHPEIEFFLLKPGPEDGSVPVPVDNAGYFDQAVHDSALNFRRHAIDALEFMGISVEFSHHEGAPGQQEIDLRFADALSMADNVMTFRYVIKEVALEEGARASFMPKPFGQHPGSAMHTHMSLFEGDVNAFHSADDPLQLSEVGKSFIAGILEHACEISAVTNQWVNSYKRLVQGGEAPTAASWGAANRSALVRVPMYTPHKTSSRRVEVRSPDSACNPYLTFAVLLAAGLRGVEKGYVLGPQAEDNVWDLTPEERRAMGYRELPSSLDSALRAMEASELVAEALGEHVFDFFLRNKRTEWANYRSHVTPYELRTYLSL
Mass: 49,608 Da
Length: 446 Aa

Rv2222c doesn't seem to be a targeted by any drug.

Two-component system mtu02020
mtu02020
Environmental Information Processing; Signal transduction

Arginine biosynthesis mtu00220
mtu00220
PATHWAY_MAP mtu00220 Arginine biosynthesis

Glyoxylate and dicarboxylate metabolism mtu00630
mtu00630
PATHWAY_MAP mtu00630 Glyoxylate and dicarboxylate metabolism

Nitrogen metabolism mtu00910
mtu00910
Metabolism; Energy metabolism

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.