Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O68427 (TRPC_BUCDN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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
Synonyms:trpC/F
OrganismBuchnera aphidicola subsp. Diuraphis noxia
Taxonomic identifier118101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length453 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.

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-Rule MF_00134_B
PRO_0000154274

Regions

Region1 – 257257Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region258 – 453196N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
O68427 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF038565 Genomic DNA. Translation: AAC27734.1.

3D structure databases

ProteinModelPortalO68427.
SMRO68427. Positions 3-260.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_BUCDN
AccessionPrimary (citable) accession number: O68427
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 67 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