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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.

Pathway:iL-tryptophan biosynthesis

This protein is involved in step 3 and 4 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Anthranilate synthase component 2 (trpG), Anthranilate synthase component 1 (trpE)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Decarboxylase, Isomerase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-282-MONOMER.
UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan biosynthesis protein TrpCF
Including the following 2 domains:
Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
Short name:
IGPS
N-(5'-phospho-ribosyl)anthranilate isomerase (EC:5.3.1.24)
Short name:
PRAI
Gene namesi
Name:trpC
Synonyms:trpC/F
Ordered Locus Names:BUsg_268
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tryptophan biosynthesis protein TrpCFPRO_0000154272Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi198804.BUsg268.

Structurei

3D structure databases

ProteinModelPortaliP42393.
SMRiP42393. Positions 3-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 256256Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni257 – 451195N-(5'-phosphoribosyl)anthranilate isomeraseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the TrpC family.Curated
In the C-terminal section; belongs to the TrpF family.Curated

Phylogenomic databases

eggNOGiCOG0134.
KOiK13498.
OMAiSFILECK.
OrthoDBiEOG6WT8JX.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQETILNKII KDKIDWIKYR KKIQPLIKFK NKINKETRNF YNSLKEKRPF
60 70 80 90 100
FILECKKSSP SLGIIRKKFN LIEIANIYKN YASAISVLTD EKYFHGNIEY
110 120 130 140 150
INVVRRCVSQ PILCKDFFID SYQVYLARYY SADAILLMLS VLNDSQYLEL
160 170 180 190 200
SRIAKELNMG VLTEINNIKE LKRAIKLNAS VIGINNRNLH DLSIDLNRTR
210 220 230 240 250
TLSPLIKNKI IVSESGIKKN HQIKELSNIV HGFLIGSSLM YRTNLETNIK
260 270 280 290 300
SLIIGDNKVC GLTRIIDAKI VESCGAVYGG LIFADNSLRK TNEKIAEKMI
310 320 330 340 350
FENNLRFIGV FQNQDIEKIV NIAQRLSLYA VQLHGSENQK YINILRKKLC
360 370 380 390 400
KKIKIWKAFS IQSTLPLLNW DHIDKYIFDS GSGGTNKTFN WSILKGSILE
410 420 430 440 450
NVILAGGINT DNVLIASQLN CSGLDFNSGV EKSPGIKDHK KISLIFKKLT

F
Length:451
Mass (Da):51,594
Last modified:November 1, 1995 - v1
Checksum:i88FD5F0E84FA7B71
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19055 Genomic DNA. Translation: CAA79499.1.
AE013218 Genomic DNA. Translation: AAM67826.1.
PIRiB49897.
RefSeqiWP_011053793.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67826; AAM67826; BUsg_268.
KEGGibas:BUsg268.
PATRICi21247341. VBIBucAph100086_0280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19055 Genomic DNA. Translation: CAA79499.1.
AE013218 Genomic DNA. Translation: AAM67826.1.
PIRiB49897.
RefSeqiWP_011053793.1. NC_004061.1.

3D structure databases

ProteinModelPortaliP42393.
SMRiP42393. Positions 3-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg268.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67826; AAM67826; BUsg_268.
KEGGibas:BUsg268.
PATRICi21247341. VBIBucAph100086_0280.

Phylogenomic databases

eggNOGiCOG0134.
KOiK13498.
OMAiSFILECK.
OrthoDBiEOG6WT8JX.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.
BioCyciBAPH198804:GHMG-282-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiTRPC_BUCAP
AccessioniPrimary (citable) accession number: P42393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.