Rv3607c Dihydroneopterin aldolase (EC 4.1.2.25)

Summary

Symbol Product Feature Type Start End Strand Length AA Length is TF
Rv3607c folB Dihydroneopterin aldolase (EC 4.1.2.25) CDS 4048744 4049145 - 402 133 FALSE

Rv3607c (Dihydroneopterin aldolase (EC 4.1.2.25)) is predicted to be co-regulated in modules bicluster_0135 with residual 0.54 and bicluster_0562 with residual 0.57.

This regulation is possibly mediated by two de-novo identified cis-regulatory motifs in each module with e-values , 3.10 and 2,200.00 for bicluster_0135 and 1,500.00 and 6,400.00 for bicluster_0562 respectively.

These modules are enriched for following go terms: small molecule biosynthetic process, single-organism biosynthetic process, aromatic compound biosynthetic process, heterocycle biosynthetic process, organic cyclic compound biosynthetic pro... .

This gene is found to be for growth on cholesterol.

Mutant available?:

Product (LegacyBRC) Product (RefSeq)
Probable dihydroneopterin aldolase dihydroneopterin aldolase FolB
Operon # Operon
2348 - - - - -
PATRIC Locus Tag Enzyme Name PATRIC Pathways Transcriptomics

PATRIC

Dihydroneopterin aldolase Folate biosynthesis
Locus Tuberculist Genome View

Tuberculist

Quickview
Locus Tag KEGG Pathways

KEGG

Folate biosynthesis

10
Total items in this category:  

KEGG

Metabolic pathways

601
Total items in this category:  
BioCyc Gene Page Cellular Overview Map
Link to STRING STRING Network

STRING

GI Number Protein ID Blast Conserved Domains
57117133 YP_177996.1 Run
GO:0004150

dihydroneopterin aldolase activity

dihydroneopterin aldolase activity

Details: 
Catalysis of the reaction: 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.
GO Category: 
molecular_function
1
Total items in this category:  
GO:0040007

growth

growth

Details: 
The increase in size or mass of an entire organism, a part of an organism or a cell.
GO Category: 
biological_process
621
Total items in this category:  
GO:0051260

protein homooligomerization

protein homooligomerization

Details: 
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
GO Category: 
biological_process
31
Total items in this category:  
No TFOE experiment results were found

Quantitative Proteomics Data

t-test p-value Cholesterol/Glycerol Ratio
NA NA

How essentiality calculations were done?

The relative representation of each mutant was determined by calculating the fold change (sequence reads/insertion in cholesterol divided by sequence reads/insertion in glycerol) for each gene. Statistical significance was determined by t-test. Each insertion site in each replicate sample was treated as a separate data point. The hyperbola used for defining genes specifically required for growth in cholesterol was defined by the formula, y = 3.8/x+0.7. Genes above this line are annotated as required for growth on cholesterol.

TRIP log2 fold abundance change

reports the log2 abundance fold change of each TFI strain, relative to no induction, in absence or presence of drug, averaged across experimental replicates. Also reported are the accompanying z-scores and two-sided t-test p-values for each TFI strain under each condition. Please refer to Ma et al., 2020, Nature Microbiology for more information.

p-value Untreated:
p-value INH: