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P0A632 (TRPC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Indole-3-glycerol phosphate synthase

Short name=IGPS
EC=4.1.1.48
Gene names
Name:trpC
Ordered Locus Names:Rv1611, MT1646
ORF Names:MTCY01B2.03
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP MF_00134_B

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5. HAMAP MF_00134_B

Miscellaneous

Was identified as a high-confidence drug target. HAMAP MF_00134_B

Sequence similarities

Belongs to the TrpC family.

Sequence caution

The sequence AAK45915.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Indole-3-glycerol phosphate synthase HAMAP MF_00134_B
PRO_0000154234

Regions

Compositional bias32 – 376Poly-Ala HAMAP MF_00134_B

Experimental info

Sequence conflict1641T → I in AAK45915. Ref.2

Secondary structure

.............................................. 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A632 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 9CA29D0F0FAC76C2

FASTA27228,023
        10         20         30         40         50         60 
MSPATVLDSI LEGVRADVAA REASVSLSEI KAAAAAAPPP LDVMAALREP GIGVIAEVKR 

        70         80         90        100        110        120 
ASPSAGALAT IADPAKLAQA YQDGGARIVS VVTEQRRFQG SLDDLDAVRA SVSIPVLRKD 

       130        140        150        160        170        180 
FVVQPYQIHE ARAHGADMLL LIVAALEQSV LVSMLDRTES LGMTALVEVH TEQEADRALK 

       190        200        210        220        230        240 
AGAKVIGVNA RDLMTLDVDR DCFARIAPGL PSSVIRIAES GVRGTADLLA YAGAGADAVL 

       250        260        270 
VGEGLVTSGD PRAAVADLVT AGTHPSCPKP AR 

« 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
BX842577 Genomic DNA. Translation: CAB08905.1.
AE000516 Genomic DNA. Translation: AAK45915.1. Different initiation.
PIRA70557.
RefSeqNP_216127.1. NC_000962.2.
NP_336101.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QJAX-ray1.29A1-272[»]
ProteinModelPortalP0A632.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000002848; EBMYCP00000002848; EBMYCG00000002846.
EBMYCT00000070654; EBMYCP00000068713; EBMYCG00000070649.
GeneID885294.
924603.
GenomeReviewsGene locus MT1646 in contig AE000516_GR.
Gene locus Rv1611 in contig AL123456_GR.
KEGGmtc:MT1646.
mtu:Rv1611.
PATRIC18125382. VBIMycTub22151_1806.
TIGRMT1646.

Organism-specific databases

TubercuListRv1611.

Phylogenomic databases

GeneTreeEBGT00050000017090.
HOGENOMHBG540956.
OMAVESLGMT.
PhylomeDBP0A632.
ProtClustDBPRK00278.

Family and domain databases

HAMAPMF_00134_B. IGPS_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01609.
PfamPF00218. IGPS. 1 hit.
[Graphical view]
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPC_MYCTU
AccessionPrimary (citable) accession number: P0A632
Secondary accession number(s): O06129
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 43 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families