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Search term: trpD

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nametrpD
Rv numberRv2192c
TypeCDS
FunctionTryptophan biosynthesis
ProductProbable anthranilate phosphoribosyltransferase TrpD
CommentsRv2192c, (MTCY190.03c), len: 370 aa. Probable trpD, anthranilate phosphoribosyltransferase (see citation below), similar to e.g. TRPD_LACCA|P17170, (43.2% identity in 308 aa overlap). Initiation codon uncertain, gtg at 4086 in MTCY190 favoured by homology but this has no clear ribosome binding site.
Molecular mass (Da)37707.8
Isoelectric point6.4033
Gene length (bp)1113
Protein length370
Location (kb)2455.63


Functional categoryintermediary metabolism and respiration


ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen 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).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011).
see TB knockouts/mutants availability


Coordinates
TypeStartEndOrientation
CDS24556312456743-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2192c|trpD
VALSAEGSSGGSRGGSPKAEAASVPSWPQILGRLTDNRDLARGQAAWAMDQIMTGNARPA
QIAAFAVAMTMKAPTADEVGELAGVMLSHAHPLPADTVPDDAVDVVGTGGDGVNTVNLST
MAAIVVAAAGVPVVKHGNRAASSLSGGADTLEALGVRIDLGPDLVARSLAEVGIGFCFAP
RFHPSYRHAAAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFADLAEVMAGVFAARRSS
VLVVHGDDGLDELTTTTTSTIWRVAAGSVDKLTFDPAGFGFARAQLDQLAGGDAQANAAA
VRAVLGGARGPVRDAVVLNAAGAIVAHAGLSSRAEWLPAWEEGLRRASAAIDTGAAEQLL
ARWVRFGRQI
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP66992
Protein Data Bank1ZVW 2BPQ 3QR9


Orthologs/Cross-references
CDC1551MT2248
Enzyme Classification2.4.2.18
Gene Ontologytryptophan biosynthetic process
anthranilate phosphoribosyltransferase activity
M. bovisMb2215c
M. lepraeML0883
M. marinumMMAR_3236
M. smegmatisMSMEG_4258
UniProtP66992
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2192c


Expression Data
TBDBRv2192c


Bibliography
Parish T, Gordhan BG, McAdam RA, Duncan K, Mizrahi V, Stoker NG,
Production of mutants in amino acid biosynthesis genes of Mycobacterium tuberculosis by homologous recombination
Microbiology (1999) 145(Pt 12):3497-503
Cited for: Mutant
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J,
The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate.
J Mol Biol (2006) 355(4):784-97
Cited for: Structure
Malen H, Berven FS, Fladmark KE, Wiker HG,
Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv.
Proteomics (2007) 7(10):1702-18
Cited for: Proteomics
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant