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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Buchnera aphidicola subsp. Diuraphis noxia
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.

Pathwayi: L-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 1 (trpE), Anthranilate synthase component 1 (trpE)
  2. Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Bifunctional indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase (ATN01_01385), Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA)
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

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
OrganismiBuchnera aphidicola subsp. Diuraphis noxia
Taxonomic identifieri118101 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001542741 – 453Tryptophan biosynthesis protein TrpCFAdd BLAST453

Structurei

3D structure databases

ProteinModelPortaliO68427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 257Indole-3-glycerol phosphate synthaseAdd BLAST257
Regioni258 – 453N-(5'-phosphoribosyl)anthranilate isomeraseAdd BLAST196

Sequence similaritiesi

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

Family and domain databases

CDDicd00331. IGPS. 1 hit.
cd00405. PRAI. 1 hit.
Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B. 1 hit.
MF_00135. PRAI. 1 hit.
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.

O68427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKETILEKIV KNKYEWIKFR KKKQPLITFK NHINTKTRNF YNSLKEKNPV
60 70 80 90 100
FILECKKKSP SLGIIKKNFN LIDIAKIYNK YASAISVLTD EKYFDGKLEF
110 120 130 140 150
INIVRERVSQ PILCKDFFID PFQIYLARYY NADAILLMLS ILDDFQYQKL
160 170 180 190 200
SKIAKELNMG ILTEVNNTSE LKRAIKLNAN IIGINNRNLH DLSINLNRTR
210 220 230 240 250
ILSSLIPKNI IIISESGITK YKQIRYLSQF VNGFLIGSHL MSEKQLEIGV
260 270 280 290 300
RSLILGENKI CGLTRSCDIE IAEKYGAVYG GLIFAPSSLR KISKNTAKKI
310 320 330 340 350
IFNNTLRNVG VFQNENIEIV KNIAEELNLY AVQLHGQEDQ KYVKKLRQTL
360 370 380 390 400
SINIQIWKAF SIDSKIPDLN WDHIHKYVLD SQFGGSNKCF NWSILKHQIL
410 420 430 440 450
ENVILAGGIN SNNCIKASKL NCSGLDLNSG IEVSPGIKDH KKIKSVFQKL

RYY
Length:453
Mass (Da):52,108
Last modified:August 1, 1998 - v1
Checksum:i4ED27374695024A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038565 Genomic DNA. Translation: AAC27734.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038565 Genomic DNA. Translation: AAC27734.1.

3D structure databases

ProteinModelPortaliO68427.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

CDDicd00331. IGPS. 1 hit.
cd00405. PRAI. 1 hit.
Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B. 1 hit.
MF_00135. PRAI. 1 hit.
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...

Entry informationi

Entry nameiTRPC_BUCDN
AccessioniPrimary (citable) accession number: O68427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 74 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

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.