Gene Rv3396c
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Involved in GMP biosynthesis [catalytic activity: ATP + xanthosine 5'-phosphate + L-glutamine + H(2)O = AMP + pyrophosphate + GMP + L-glutamate]. |
| Product | Probable GMP synthase [glutamine-hydrolyzing] GuaA (glutamine amidotransferase) (GMP synthetase) |
| Comments | Rv3396c, (MTCY78.32), len: 525 aa. Probable guaA, gmp synthase (see citation below), equivalent to P46810|GUAA_MYCLE|ML0395|B1620_C2_205 GMP synthase [glutamine-hydrolyzing] from Mycobacterium leprae (529 aa), FASTA scores: opt: 2992, E(): 8.5e-168, (86.85% identity in 525 aa overlap). Also highly similar to others e.g. O52831|GUAA_CORAM from Corynebacterium ammoniagenes (Brevibacterium ammoniagenes) (524 aa), FASTA scores: opt: 2636, E(): 5.9e-147, (76.2% identity in 521 aa overlap); Q9L0H2|GUAA_STRCO from Streptomyces coelicolor (526 aa), FASTA scores: opt: 2451, E(): 4.1e-136, (71.55% identity in 513 aa overlap); Q9KF78|GUAA_BACHD from Bacillus Halodurans (513 aa), FASTA scores: opt: 1819, E(): 4.1e-99, (52.55% identity in 510 aa overlap); etc. Contains PS00442 Glutamine amidotransferases class-I active site. Belongs to the type-1 glutamine amidotransferase family in the N-terminal section. And belongs to the GMP synthase family in the C-terminal section. |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | Identified by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (See Jungblut et al., 1999). Detected by 2-DE and MS in M. tuberculosis H37Rv purified from phagosomes of infected murine bone marrow macrophages but not in H37Rv broth-cultures (See Mattow et al., 2006). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011). |
| Mutant | Essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 3812501 | 3814078 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3396c|guaA
VVQPADIDVPETPARPVLVVDFGAQYAQLIARRVREARVFSEVIPHTASIEEIRARQPVALVLSGGPASVYADGAPKLDPALLDLGVPVLGICYGFQAMAQALGGIVAHTGTREYGRTELKVLGGKLHSDLPEVQPVWMSHGDAVTAAPDGFDVVASSAGAPVAAFEAFDRRLAGVQYHPEVMHTPHGQQVLSRFLHDFAGLGAQWTPANIANALIEQVRTQIGDGHAICGLSGGVDSAVAAALVQRAIGDRLTCVFVDHGLLRAGERAQVQRDFVAATGANLVTVDAAETFLEALSGVSAPEGKRKIIGRQFIRAFEGAVRDVLDGKTAEFLVQGTLYPDVVESGGGSGTANIKSHHNVGGLPDDLKFTLVEPLRLLFKDEVRAVGRELGLPEEIVARQPFPGPGLGIRIVGEVTAKRLDTLRHADSIVREELTAAGLDNQIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRVPYEVLERISTRITNEVAEVNRVVLDITSKPPATIEWE
Bibliography
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Kamalakannan V et al. [2002]. Identification of a novel mycobacterial transcriptional regulator and its involvement in growth rate dependence and stringent control. Sequence Regulation
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Mattow J, Siejak F, Hagens K, Becher D, Albrecht D, Krah A, Schmidt F, Jungblut PR, Kaufmann SH and Schaible UE [2006]. Proteins unique to intraphagosomally grown Mycobacterium tuberculosis. Proteomics
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
