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Reviewed, UniProtKB/Swiss-Prot P42393 (TRPC_BUCAP)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names: BUsg_268
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length451 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.

Subunit structure

Monomer By similarity.

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 – 451451Tryptophan biosynthesis protein trpCF HAMAP MF_00134
PRO_0000154272

Regions

Region1 – 256256Indole-3-glycerol phosphate synthase HAMAP MF_00134
Region257 – 451195N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Sequences

Sequence LengthMass (Da)Tools
P42393-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 88FD5F0E84FA7B71

FASTA45151,594
        10         20         30         40         50         60 
MQETILNKII KDKIDWIKYR KKIQPLIKFK NKINKETRNF YNSLKEKRPF FILECKKSSP 

        70         80         90        100        110        120 
SLGIIRKKFN LIEIANIYKN YASAISVLTD EKYFHGNIEY INVVRRCVSQ PILCKDFFID 

       130        140        150        160        170        180 
SYQVYLARYY SADAILLMLS VLNDSQYLEL SRIAKELNMG VLTEINNIKE LKRAIKLNAS 

       190        200        210        220        230        240 
VIGINNRNLH DLSIDLNRTR TLSPLIKNKI IVSESGIKKN HQIKELSNIV HGFLIGSSLM 

       250        260        270        280        290        300 
YRTNLETNIK SLIIGDNKVC GLTRIIDAKI VESCGAVYGG LIFADNSLRK TNEKIAEKMI 

       310        320        330        340        350        360 
FENNLRFIGV FQNQDIEKIV NIAQRLSLYA VQLHGSENQK YINILRKKLC KKIKIWKAFS 

       370        380        390        400        410        420 
IQSTLPLLNW DHIDKYIFDS GSGGTNKTFN WSILKGSILE NVILAGGINT DNVLIASQLN 

       430        440        450 
CSGLDFNSGV EKSPGIKDHK KISLIFKKLT F 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequence of a putative trpDC(F)BA operon in Buchnera aphidicola (endosymbiont of the aphid Schizaphis graminum)."
Munson M.A., Baumann P.
J. Bacteriol. 175:6426-6432(1993) [PubMed: 8407819] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

Z19055 Genomic DNA. Translation: CAA79499.1.
AE013218 Genomic DNA. Translation: AAM67826.1.
PIRB49897.
RefSeqNP_660615.1.

3D structure databases

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

Genome annotation databases

GeneID1005470.
GenomeReviewsGene locus BUsg_268 in contig AE013218_GR.
KEGGbas:BUsg268.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP42393.
OMAYILECKK.

Enzyme and pathway databases

BioCycBAPH198804:BUSG268-MON.

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_BUCAP
AccessionPrimary (citable) accession number: P42393
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 3, 2009
This is version 64 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

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