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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 4 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 1 (trpE), Anthranilate synthase component 2 (trpG)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Indole-3-glycerol phosphate synthase (Cgl2091), 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

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:trpCF
Ordered Locus Names:Cgl3033, cg3362
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
ProteomesiUP000000582 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Tryptophan biosynthesis protein TrpCFPRO_0000154276Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi196627.cg3362.

Structurei

3D structure databases

ProteinModelPortaliP06560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 262262Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni263 – 474212N-(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_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.

P06560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSNNLPTVL ESIVEGRRGH LEEIRARIAH VDVDALPKST RSLFDSLNQG
60 70 80 90 100
RGGARFIMEC KSASPSLGMI REHYQPGEIA RVYSRYASGI SVLCEPDRFG
110 120 130 140 150
GDYDHLATVA ATSHLPVLCK DFIIDPVQVH AARYFGADAI LLMLSVLDDE
160 170 180 190 200
EYAALAAEAA RFDLDILTEV IDEEEVARAI KLGAKIFGVN HRNLHDLSID
210 220 230 240 250
LDRSRRLSKL IPADAVLVSE SGVRDTETVR QLGGHSNAFL VGSQLTSQEN
260 270 280 290 300
VDLAARELVY GPNKVCGLTS PSAAQTARAA GAVYGGLIFE EASPRNVSRE
310 320 330 340 350
TLQKIIAAEP NLRYVAVSRR TSGYKDLLVD GIFAVQIHAP LQDSVEAEKA
360 370 380 390 400
LIAAVREEVG PQVQVWRAIS MSSPLGAEVA AAVEGDVDKL ILDAHEGGSG
410 420 430 440 450
EVFDWATVPA AVKAKSLLAG GISPDNAAQA LAVGCAGLDI NSGVEYPAGA
460 470
GTWAGAKDAG ALLKIFATIS TFHY
Length:474
Mass (Da):50,477
Last modified:July 26, 2002 - v2
Checksum:iC347C7016BB97F9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 892SG → AA in CAA28626 (PubMed:3808947).Curated
Sequence conflicti110 – 1101A → G in CAA28626 (PubMed:3808947).Curated
Sequence conflicti130 – 1312HA → RP in CAA28626 (PubMed:3808947).Curated
Sequence conflicti153 – 1531A → D in CAA28626 (PubMed:3808947).Curated
Sequence conflicti302 – 3021L → S in CAA28626 (PubMed:3808947).Curated
Sequence conflicti343 – 3431D → G in CAA28626 (PubMed:3808947).Curated
Sequence conflicti381 – 3833Missing in CAA28626 (PubMed:3808947).Curated
Sequence conflicti454 – 47421AGAKD…STFHY → GWGERCRRAAENFRDHLHIP LLKV in CAA28626 (PubMed:3808947).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04960 Genomic DNA. Translation: CAA28626.1.
BA000036 Genomic DNA. Translation: BAC00427.1.
BX927157 Genomic DNA. Translation: CAF18973.1.
PIRiE24723.
RefSeqiNP_602226.2. NC_003450.3.
WP_011015582.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAC00427; BAC00427; BAC00427.
CAF18973; CAF18973; cg3362.
GeneIDi1020975.
KEGGicgb:cg3362.
cgl:NCgl2930.
PATRICi21498118. VBICorGlu203724_2967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04960 Genomic DNA. Translation: CAA28626.1.
BA000036 Genomic DNA. Translation: BAC00427.1.
BX927157 Genomic DNA. Translation: CAF18973.1.
PIRiE24723.
RefSeqiNP_602226.2. NC_003450.3.
WP_011015582.1. NC_006958.1.

3D structure databases

ProteinModelPortaliP06560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg3362.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC00427; BAC00427; BAC00427.
CAF18973; CAF18973; cg3362.
GeneIDi1020975.
KEGGicgb:cg3362.
cgl:NCgl2930.
PATRICi21498118. VBICorGlu203724_2967.

Phylogenomic databases

eggNOGiCOG0134.
KOiK13498.
OMAiSFILECK.
OrthoDBiEOG6WT8JX.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_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. "Complete nucleotide and deduced amino acid sequences of the Brevibacterium lactofermentum tryptophan operon."
    Matsui K., Sano K., Ohtsubo E.
    Nucleic Acids Res. 14:10113-10114(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiTRPC_CORGL
AccessioniPrimary (citable) accession number: P06560
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 26, 2002
Last modified: July 22, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.