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Q44603 (TRPC_BUCSC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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. Schlechtendalia chinensis
Taxonomic identifier118110 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length461 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 – 461461Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154275

Regions

Region1 – 258258Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region259 – 461203N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
Q44603 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09185 Genomic DNA. Translation: AAA92795.1.

3D structure databases

ProteinModelPortalQ44603.
SMRQ44603. Positions 3-261.
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_BUCSC
AccessionPrimary (citable) accession number: Q44603
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 71 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