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P59459 (TRPC_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

  1. Indole-3-glycerol phosphate synthase
    Short name=IGPS
    EC=4.1.1.48
  2. N-(5'-phospho-ribosyl)anthranilate isomerase
    Short name=PRAI
    EC=5.3.1.24
Gene names
Name:trpC
Ordered Locus Names:bbp_259
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain By similarity. HAMAP-Rule MF_00134_B

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B

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

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00134_B

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00134_B

Sequence similarities

In the N-terminal section; belongs to the TrpC family.

In the C-terminal section; belongs to the TrpF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154273

Regions

Region1 – 257257Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region258 – 469212N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
P59459 [UniParc].

Last modified March 28, 2003. Version 1.
Checksum: 089802BE9F178FD9

FASTA46954,239
        10         20         30         40         50         60 
MNSILKEIIN DKLMWVKYHK KKQPLFTFQN KIVRSNYNFK NSLKSIHPSY ILEIKKASPS 

        70         80         90        100        110        120 
LGIINNKLDL KKISLIYKKY ASSISILTDE KYFHGNFEFI PIVRKIAHRQ PILCKDFFID 

       130        140        150        160        170        180 
PYQIYLARYY QADAILLMLS ILNDNQYVFL RNIAEMLNMD VLTEIENKKE LTRAINLKSK 

       190        200        210        220        230        240 
IIGINNRNLN NLSIDIQKTK VLAPLIPKKI IIISESGIQN YNQIRQLKPF VQGFLIGSNL 

       250        260        270        280        290        300 
MRKKNLEEAV CKMILGNNKI CGLTQSSDVK IIKEYGIVYG GLIFCKFSPR YINCNNAYSI 

       310        320        330        340        350        360 
INNVSLKYIG VFCNENLKRV AYIGTKLSLH AVQLHGNEDQ IYINNLKLIL PKHIKIWKSI 

       370        380        390        400        410        420 
IYLDFLKNQK HLFYNVNKYI IDNKDGGSGK TFNWKYLKNC KLDNVILAGG LDINNCILAT 

       430        440        450        460 
DLGCYGYDFN SKLESSPGIK DLKKIVALTY SLRRHTVFNY RNLICLGKK 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26986.1.
RefSeqNP_777881.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59459.
SMRP59459. Positions 1-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26986; AAO26986; bbp_259.
GeneID1058465.
KEGGbab:bbp259.
PATRIC21245299. VBIBucAph80364_0252.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0134.
KOK13498.
OMASFILECK.
OrthoDBEOG6WT8JX.
ProtClustDBPRK09427.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-259-MONOMER.
UniPathwayUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 2 hits.
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPC_BUCBP
AccessionPrimary (citable) accession number: P59459
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: February 19, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways