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fabG1 3-oxoacyl-ACP reductase FabG [ Mycobacterium tuberculosis H37Rv ]

Gene ID: 886551, updated on 6-Oct-2023

Summary

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Gene symbol
fabG1
Gene description
3-oxoacyl-ACP reductase FabG
Locus tag
Rv1483
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Mycobacterium tuberculosis H37Rv (strain: H37Rv, type-material: type strain of Mycobacterium tuberculosis)
Lineage
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex
Also known as
mabA
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Genomic context

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Sequence:
NC_000962.3 (1673440..1674183)

NC_000962.3Genomic Context describing neighboring genes Neighboring gene membrane protein Neighboring gene hypothetical protein Neighboring gene NADH-dependent enoyl-[ACP] reductase Neighboring gene ferrochelatase Neighboring gene hypothetical protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000962.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Evaluation of the potential role of a new mutation in mabA in modifying the response of Mycobacterium tuberculosis to isoniazid. Alonso M, et al. Tuberculosis (Edinb), 2013 Nov. PMID 23973657
  2. Crystallization and preliminary X-ray diffraction analysis of the high molecular weight ketoacyl reductase FabG4 complexed with NADH. Dutta D, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012 Jul 1. PMID 22750865, Free PMC Article
  3. Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies. Poncet-Montange G, et al. Acta Crystallogr D Biol Crystallogr, 2007 Aug. PMID 17642518
  4. A silent mutation in mabA confers isoniazid resistance on Mycobacterium tuberculosis. Ando H, et al. Mol Microbiol, 2014 Feb. PMID 24354762
  5. Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-ketoacyl-ACP Reductase (MabA). Rosado LA, et al. BMC Res Notes, 2012 Sep 25. PMID 23006410, Free PMC Article

See all (12) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. study identified the mabA(g609a) silent mutation in a significant number of isoniazid (INH)resistant Mtb clinical isolates without known INH resistance mutations; findings show here that the mabA(g609a) mutation resulted in the upregulation of inhA
    Title: A silent mutation in mabA confers isoniazid resistance on Mycobacterium tuberculosis.
  2. a new mutation in mabA, Thr4Ile, was identified; a putative role for this mutation in the process of diminishing susceptibility to isoniazid is evaluated
    Title: Evaluation of the potential role of a new mutation in mabA in modifying the response of Mycobacterium tuberculosis to isoniazid.
  3. Data suggest that a better understanding of the mode of action of beta-ketoacyl-ACP Reductase (MabA) should be useful to guide the rational (function-based) design of inhibitors of MabA enzyme activity and used as lead compounds with anti-TB action.
    Title: Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-ketoacyl-ACP Reductase (MabA).
  4. A mountable FabG4:NADH complex crystal diffracted to 2.59 A resolution and belonged to space group P1, with unit-cell parameters a = 63.07, b = 71.03, c = 92.92 A, alpha = 105.02, beta = 97.06, gamma = 93.66 degrees
    Title: Crystallization and preliminary X-ray diffraction analysis of the high molecular weight ketoacyl reductase FabG4 complexed with NADH.
  5. The essential mycobacterial genes, fabG1 and fabG4, encode 3-oxoacyl-thioester reductases that are functional in yeast mitochondrial fatty acid synthase type 2.
    Title: The essential mycobacterial genes, fabG1 and fabG4, encode 3-oxoacyl-thioester reductases that are functional in yeast mitochondrial fatty acid synthase type 2.
  6. A mechanism of substrate binding to MabA is proposed that indicates positive cooperativity in NADPH binding, with two forms of free enzyme present in solution, and a reduced affinity of both substrates for the monomeric form of MabA.
    Title: Mycobacterium tuberculosis beta-ketoacyl-ACP reductase: alpha-secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding.
  7. mutation (G139A) is reported that leads to complete protein inactivation and freezes the catalytic site into its closed form
    Title: Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.
  8. crystal structure of the wild-type MabA in the presence of NADP was solved and showing a mixture of the two mutually exclusive conformations
    Title: Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change.
  9. FabG1 activity can be replaced by the corresponding enzyme from the closely related species Mycobacterium smegmatis but not by the enzyme from Escherichia coli
    Title: Functional complementation of the essential gene fabG1 of Mycobacterium tuberculosis by Mycobacterium smegmatis fabG but not Escherichia coli fabG.
Submit: New GeneRIF Correction

General gene information

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Homology

General protein information

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Preferred Names
3-oxoacyl-ACP reductase FabG
NP_215999.1
  • 3-ketoacyl-acyl carrier protein reductase (mycolic acid biosynthesis a protein)

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000962.3 Reference assembly

    Range
    1673440..1674183
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_215999.1 3-oxoacyl-ACP reductase FabG [Mycobacterium tuberculosis H37Rv]

    See identical proteins and their annotated locations for NP_215999.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A2I7W6M7
    Conserved Domains (1) summary
    cd05333
    Location:16 → 244
    BKR_SDR_c; beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P9WGT3.1

Gene LinkOut

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Molecular Biology Databases
Research Materials