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Reviewed, UniProtKB/Swiss-Prot O68427 (TRPC_BUCDN)

Last modified March 3, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tryptophan biosynthesis protein trpCF
Including the following 2 domains:
    1- Recommended name:
            Indole-3-glycerol phosphate synthase
                Short name=IGPS
              EC=4.1.1.48
    2- Recommended name:
            N-(5'-phospho-ribosyl)anthranilate isomerase
                Short name=PRAI
              EC=5.3.1.24
Gene names
Name: trpC
Synonyms: trpC/F
OrganismBuchnera aphidicola subsp. Diuraphis noxia
Taxonomic identifier118101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. HAMAP MF_00134

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP MF_00134

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP MF_00134

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP MF_00134

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

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 – 453453Tryptophan biosynthesis protein trpCF HAMAP MF_00134
PRO_0000154274

Regions

Region1 – 257257Indole-3-glycerol phosphate synthase HAMAP MF_00134
Region258 – 453196N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Sequences

Sequence LengthMass (Da)Tools
O68427-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 4ED27374695024A5

FASTA45352,108
        10         20         30         40         50         60 
MKETILEKIV KNKYEWIKFR KKKQPLITFK NHINTKTRNF YNSLKEKNPV FILECKKKSP 

        70         80         90        100        110        120 
SLGIIKKNFN LIDIAKIYNK YASAISVLTD EKYFDGKLEF INIVRERVSQ PILCKDFFID 

       130        140        150        160        170        180 
PFQIYLARYY NADAILLMLS ILDDFQYQKL SKIAKELNMG ILTEVNNTSE LKRAIKLNAN 

       190        200        210        220        230        240 
IIGINNRNLH DLSINLNRTR ILSSLIPKNI IIISESGITK YKQIRYLSQF VNGFLIGSHL 

       250        260        270        280        290        300 
MSEKQLEIGV RSLILGENKI CGLTRSCDIE IAEKYGAVYG GLIFAPSSLR KISKNTAKKI 

       310        320        330        340        350        360 
IFNNTLRNVG VFQNENIEIV KNIAEELNLY AVQLHGQEDQ KYVKKLRQTL SINIQIWKAF 

       370        380        390        400        410        420 
SIDSKIPDLN WDHIHKYVLD SQFGGSNKCF NWSILKHQIL ENVILAGGIN SNNCIKASKL 

       430        440        450 
NCSGLDLNSG IEVSPGIKDH KKIKSVFQKL RYY 

« Hide

References

[1]"The endosymbiont (Buchnera) of the aphid Diuraphis noxia contains all the genes of the tryptophan biosynthetic pathway."
Baumann L., Baumann P., Moran N.A.
Curr. Microbiol. 37:58-59(1998) [PubMed: 9625791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AF038565 Genomic DNA. Translation: AAC27734.1.

3D structure databases

HSSPHSSP built from PDB template 1JCM based on UniProtKB P00909.
ModBaseSearch...

Family and domain databases

HAMAPMF_00134. Fused.
[Tree]
MF_00135. Fused.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GPS_central.
IPR001240. PRAI.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
ProDomPD001511. IGPS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPC_BUCDN
AccessionPrimary (citable) accession number: O68427
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: March 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents