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Q9PGT5 (TRPC_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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:
Indole-3-glycerol phosphate synthase

Short name=IGPS
EC=4.1.1.48
Gene names
Name:trpC
Ordered Locus Names:XF_0213
OrganismXylella fastidiosa [Complete proteome] [HAMAP]
Taxonomic identifier2371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Sequence similarities

Belongs to the TrpC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Indole-3-glycerol phosphate synthase HAMAP MF_00134_B
PRO_0000154269

Sequences

Sequence LengthMass (Da)Tools
Q9PGT5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 86E388A910EB30B0

FASTA26428,700
        10         20         30         40         50         60 
MSNILTKIIA WKVEEIAERL LHVSQAELVA RCADLPTPRG FAGALQATIA HGDPAVIAEI 

        70         80         90        100        110        120 
KKASPSKGVL REDFRPAEIA ISYELGGASC LSVLTDVHFF KGHDDYLSQA RDACTLPVLR 

       130        140        150        160        170        180 
KDFTIDPYQV YEARVLGADC ILLIVAALDD AQLVDLSGLA LQLGMDVLVE VHDIDELERA 

       190        200        210        220        230        240 
IQISAPLIGI NNRNLSTFNV SLETTLTMKG LVPRDRLLVS ESGILTSADV QRLRAAGVNA 

       250        260 
FLVGEAFMRA TEPGESLREM FFIT 

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. expand/collapse author list , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
Nature 406:151-159(2000) [PubMed: 10910347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003849 Genomic DNA. Translation: AAF83026.1.
PIRA82833.
RefSeqNP_297506.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PGT5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1125736.
GenomeReviewsGene locus XF_0213 in contig AE003849_GR.
KEGGxfa:XF0213.
NMPDRfig|160492.1.peg.213.
PATRIC24130347. VBIXylFas578_0225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG540956.
OMAFETDINT.
ProtClustDBPRK00278.

Enzyme and pathway databases

BioCycXFAS160492:XF0213-MONOMER.

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_XYLFA
AccessionPrimary (citable) accession number: Q9PGT5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 62 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