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Reviewed, UniProtKB/Swiss-Prot Q44603 (TRPC_BUCSC)

Last modified May 5, 2009. Version 51. 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. Schlechtendalia chinensis
Taxonomic identifier118110 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length461 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 – 461461Tryptophan biosynthesis protein trpCF HAMAP MF_00134
PRO_0000154275

Regions

Region1 – 258258Indole-3-glycerol phosphate synthase HAMAP MF_00134
Region259 – 461203N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Sequences

Sequence LengthMass (Da)Tools
Q44603-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F202C81D6419D68D

FASTA46152,784
        10         20         30         40         50         60 
MVLENILEKI VKSKINWIKH RKKIQPLSSF QHNITLSDRN FIQALKNIHP ALILEFKKHS 

        70         80         90        100        110        120 
PSLGILNDFN PEFVAKIYKK YASAISVLTD EKYFHGKFEF IPIIRNIAVQ QPILCKDFFI 

       130        140        150        160        170        180 
DPYQIYLARY YQADSILLML SILKDNQYRA LEKLAYSLNM AVLTEINNKM ELDRAINLNA 

       190        200        210        220        230        240 
KIIGINNRNL KNFSISTSNT YKLASKISKN TIVISESGIN SYNQLRKFKN LVQGFLIGSA 

       250        260        270        280        290        300 
LMSKKDLEHA VHKIITGNNK ICGLTRVEDA RMSKDFGAIY GGFIFCKSSK RYVNLKKAMN 

       310        320        330        340        350        360 
ITKNVHMKYI GVFCNENIST ISYIIDKIPL YAIQLHGNEN QFYIDCLKKK IPKCVRVWKA 

       370        380        390        400        410        420 
ISLNGEKKHA NNLFDNVNKH VFDNIHGGSG TPFNWYLLKN YNLKNVILAG GLNIKNCISA 

       430        440        450        460 
SDLGCFGLDF NSGIEISPGL KDKKKTFLIF RSLREHKTII H 

« Hide

References

[1]"Genetics of the tryptophan biosynthetic pathway of the prokaryotic endosymbiont (Buchnera) of the aphid Schlechtendalia chinensis."
Lai C.-Y., Baumann P., Moran N.A.
Insect Mol. Biol. 4:47-59(1995) [PubMed: 7742976] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

U09185 Genomic DNA. Translation: AAA92795.1.

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_BUCSC
AccessionPrimary (citable) accession number: Q44603
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 5, 2009
This is version 51 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