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Q7DAK6 (TRPG_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Anthranilate synthase component 2

EC=4.1.3.27
Alternative name(s):
Anthranilate synthase component II
Glutamine amido-transferase
Gene names
Name:trpG
Ordered Locus Names:Rv0013, MT0016
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.

Subunit structure

Tetramer of two components I and two components II By similarity.

Miscellaneous

Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity By similarity.

Was identified as a high-confidence drug target.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Anthranilate synthase component 2
PRO_0000390894

Regions

Domain2 – 198197Glutamine amidotransferase type-1

Sites

Active site831 By similarity
Active site1721 By similarity
Active site1741 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7DAK6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A074EA1C2681AC0D

FASTA23224,627
        10         20         30         40         50         60 
MRILVVDNYD SFVFNLVQYL GQLGIEAEVW RNDDHRLSDE AAVAGQFDGV LLSPGPGTPE 

        70         80         90        100        110        120 
RAGASVSIVH ACAAAHTPLL GVCLGHQAIG VAFGATVDRA PELLHGKTSS VFHTNVGVLQ 

       130        140        150        160        170        180 
GLPDPFTATR YHSLTILPKS LPAVLRVTAR TSSGVIMAVQ HTGLPIHGVQ FHPESILTEG 

       190        200        210        220        230 
GHRILANWLT CCGWTQDDTL VRRLENEVLT AISPHFPTST ASAGEATGRT SA 

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842572 Genomic DNA. Translation: CAE55234.1.
AE000516 Genomic DNA. Translation: AAK44238.1.
PIRC70699.
RefSeqNP_334424.1. NC_002755.2.
YP_177615.1. NC_000962.2.

3D structure databases

ProteinModelPortalQ7DAK6.
ModBaseSearch...

Protein family/group databases

MEROPSC26.A19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000000103; EBMYCP00000000103; EBMYCG00000000103.
EBMYCT00000070459; EBMYCP00000068518; EBMYCG00000070454.
GeneID885955.
922462.
GenomeReviewsGene locus MT0016 in contig AE000516_GR.
Gene locus Rv0013 in contig AL123456_GR.
KEGGmtc:MT0016.
mtu:Rv0013.
PATRIC18121762. VBIMycTub22151_0017.
TIGRMT0016.

Organism-specific databases

TubercuListRv0013.

Phylogenomic databases

GeneTreeEBGT00050000015859.
HOGENOMHBG292341.
OMAEDSTIMA.
PhylomeDBQ7DAK6.
ProtClustDBPRK07765.

Family and domain databases

InterProIPR017926. GATASE_1.
IPR006221. TrpG_papA.
[Graphical view]
KOK01664.
PfamPF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00566. TrpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPG_MYCTU
AccessionPrimary (citable) accession number: Q7DAK6
Secondary accession number(s): Q79G16
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families