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Gene: trpG

General annotation | Coordinates | Sequence | Genome Browser | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography


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General annotation
Gene nametrpG
Rv numberRv0013
Synonym(s)pabA
TypeCDS
FunctionPOSSIBLY INVOLVED IN BIOSYNTHESIS OF TRYPTOPHAN (AT THE FIRST STEP). SUPPOSED TETRAMER OF TWO COMPONENTS I AND TWO COMPONENTS II: COMPONENT I (Rv1609|trpE) CATALYZES THE FORMATION OF ANTHRANILATE USING AMMONIA RATHER THAN GLUTAMINE, WHEREAS COMPONENT II (Rv0013|trpG) PROVIDES GLUTAMINE AMIDOTRANSFERASE ACTIVITY. POSSIBLY PARTICIPATES IN THE TRYPTOPHAN-DEPENDENT INDOLE-3-ACETIC ACID PRODUCTION [CATALYTIC ACTIVITY: CHORISMATE + L-GLUTAMINE = ANTHRANILATE + PYRUVATE + L-GLUTAMATE].
ProductPOSSIBLE ANTHRANILATE SYNTHASE COMPONENT II TRPG (GLUTAMINE AMIDOTRANSFERASE)
Evidenceexperimental
CommentsRv0013, (MTCY10H4.13), len: 232 aa. Possible trpG, anthranilate synthase component II (glutamine amidotransferase) , equivalent to NP_301141.1|NC_002677 putative p-aminobenzoate synthase glutamine amidotransferase from Mycobacterium leprae (232 aa). Also highly similar to others e.g. P26922|TRPG_AZOBR Anthranilate synthase component II from Azospirillum brasilense (196 aa), FASTA scores: opt: 703, E(): 8.6e-40, (56.7% identity in 187 aa overlap); T36720 probable glutamine amidotransferase from Streptomyces coelicolor (212 aa); T44524 anthranilate synthase from Nitrosomonas europaea (199 aa); etc. Also similar to E235740 para-aminobenzoate synthase (232 aa), FASTA scores: opt: 1273, E(): 0, (79.7% identity in 232 aa overlap). Contains PS00606 Beta-ketoacyl synthases active site; and PS00442 Glutamine amidotransferases class-I active site. SIMILARITY TO OTHER TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAINS. Note that previously known as pabA.
Molecular mass (Da)24626.9
Isoelectric point6.5024
Gene length (bp)699
Protein length232
Location (kb)14.914


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).
TranscriptomemRNA identified by microarray analysis and down-regulated after 96h of starvation (see Betts et al., 2002).
Annotation Changesproteomics updated on 01-APR-2009


Coordinates
TypeStartEndOrientation
CDS1491415612+


Protein sequence in FASTA format
>M. tuberculosis H37Rv | trpG
MRILVVDNYDSFVFNLVQYLGQLGIEAEVWRNDDHRLSDEAAVAGQFDGVLLSPGPGTPERAGASVSIVHACAAAHTPLL
GVCLGHQAIGVAFGATVDRAPELLHGKTSSVFHTNVGVLQGLPDPFTATRYHSLTILPKSLPAVLRVTARTSSGVIMAVQ
HTGLPIHGVQFHPESILTEGGHRILANWLTCCGWTQDDTLVRRLENEVLTAISPHFPTSTASAGEATGRTSA
Blastp: results
TransMembrane prediction using Hidden Markov Models: tmhmm
Microbe Genome Browser
Genomic sequence

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



Structural information
Protein Data BankNo structure available
PFAMProtein Family Domains


Orthologs/Cross-references
CDC1551MT0016
Enzyme Classification4.1.3.27
Gene Ontologyanthranilate synthase activity
glutamine metabolic process
biosynthetic process
transferase activity
MbovisMb0013
MlepraeML0015
MsmegmatisMSMEG_0029
UniProtQ7DAK6


Interacting Drugs/Compounds
TDR TargetsRv0013


Expression Data
TBDBRv0013


Bibliography
Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K,
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
Mol Microbiol (2002) 43 :717
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