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P57366 (TRPC_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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:
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
Ordered Locus Names:BU279
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [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.

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 – 453453Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154271

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
P57366 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 25F506D52614D9E5

FASTA45352,065
        10         20         30         40         50         60 
MQDTTLKKII QDKSEWIRLR KEKQPLIDFK DKINKKTRDF YHSLKEKKPC FILEYKKKSP 

        70         80         90        100        110        120 
SLGIIRNNFN LIEISNVYKK YASSVSVLTD EKYFHGNLNF INIVRECVSQ PVLCKDFFID 

       130        140        150        160        170        180 
PYQVYLSRYY NADAILLMLS VLNDIQYKEL SIIAKKLNMG ILTEVNNIEE LKRALKLNAN 

       190        200        210        220        230        240 
IIGINNRNLH DLSIDLNRTR TLSSLIKKDT IIISESGIKK YREIKELSKF VNGFLIGSHL 

       250        260        270        280        290        300 
MSQTNLETAV RSIIFGDNKV CGLTRSIDIE VSEKYGAIYG GLIFVKNSPR YITKKTAKNI 

       310        320        330        340        350        360 
SINRKLKLIG IFQNENINII VDIAEELSLY GVQLHGQENK QYIDKLRNIL PKKINIWKAF 

       370        380        390        400        410        420 
SIQSELPDRN WDNVNMYIFD SDSGGSNTSF NWSILNHHIL DNVILAGGIN LKNCITASKL 

       430        440        450 
KCSGLDLNSG VEISPGIKDY KKIKSIFQKL RYG 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB12989.1.
RefSeqNP_240103.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57366.
SMRP57366. Positions 4-260.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP57366.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB12989; BAB12989; BAB12989.
GeneID1109718.
KEGGbuc:BU279.
PATRIC21244082. VBIBucAph127364_0289.

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280458.
KOK13498.
OMASFILECK.
OrthoDBEOG6WT8JX.
ProtClustDBPRK09427.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-279-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_BUCAI
AccessionPrimary (citable) accession number: P57366
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 81 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names