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Reviewed, UniProtKB/Swiss-Prot P06560 (TRPC_CORGL)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: trpCF
Ordered Locus Names: Cgl3033, cg3362
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length474 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. HAMAP MF_00134

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 – 474474Tryptophan biosynthesis protein trpCF HAMAP MF_00134
PRO_0000154276

Regions

Region1 – 262262Indole-3-glycerol phosphate synthase HAMAP MF_00134
Region263 – 474212N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Experimental info

Sequence conflict88 – 892SG → AA in CAA28626. Ref.1
Sequence conflict1101A → G in CAA28626. Ref.1
Sequence conflict130 – 1312HA → RP in CAA28626. Ref.1
Sequence conflict1531A → D in CAA28626. Ref.1
Sequence conflict3021L → S in CAA28626. Ref.1
Sequence conflict3431D → G in CAA28626. Ref.1
Sequence conflict381 – 3833Missing in CAA28626. Ref.1
Sequence conflict454 – 47421AGAKD…STFHY → GWGERCRRAAENFRDHLHIP LLKV in CAA28626. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P06560-1 [UniParc].

Last modified July 26, 2002. Version 2.
Checksum: C347C7016BB97F9A

FASTA47450,477
        10         20         30         40         50         60 
MTSNNLPTVL ESIVEGRRGH LEEIRARIAH VDVDALPKST RSLFDSLNQG RGGARFIMEC 

        70         80         90        100        110        120 
KSASPSLGMI REHYQPGEIA RVYSRYASGI SVLCEPDRFG GDYDHLATVA ATSHLPVLCK 

       130        140        150        160        170        180 
DFIIDPVQVH AARYFGADAI LLMLSVLDDE EYAALAAEAA RFDLDILTEV IDEEEVARAI 

       190        200        210        220        230        240 
KLGAKIFGVN HRNLHDLSID LDRSRRLSKL IPADAVLVSE SGVRDTETVR QLGGHSNAFL 

       250        260        270        280        290        300 
VGSQLTSQEN VDLAARELVY GPNKVCGLTS PSAAQTARAA GAVYGGLIFE EASPRNVSRE 

       310        320        330        340        350        360 
TLQKIIAAEP NLRYVAVSRR TSGYKDLLVD GIFAVQIHAP LQDSVEAEKA LIAAVREEVG 

       370        380        390        400        410        420 
PQVQVWRAIS MSSPLGAEVA AAVEGDVDKL ILDAHEGGSG EVFDWATVPA AVKAKSLLAG 

       430        440        450        460        470 
GISPDNAAQA LAVGCAGLDI NSGVEYPAGA GTWAGAKDAG ALLKIFATIS TFHY 

« Hide

References

« Hide 'large scale' references
[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: 3808947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

X04960 Genomic DNA. Translation: CAA28626.1.
BA000036 Genomic DNA. Translation: BAC00427.1.
BX927157 Genomic DNA. Translation: CAF18973.1.
PIRE24723.
RefSeqNP_602226.2.
YP_227283.1.

3D structure databases

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

Genome annotation databases

GeneID1020975.
3345646.
GenomeReviewsGene locus Cgl3033 in contig BA000036_GR.
Gene locus cg3362 in contig BX927147_GR.
KEGGcgb:cg3362.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP06560.
OMAP06560. YILECKK.

Enzyme and pathway databases

BioCycCGLU196627-1:CG3362-MON.
BRENDA4.1.1.48. 812.
5.3.1.24. 812.

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_CORGL
AccessionPrimary (citable) accession number: P06560
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 26, 2002
Last modified: June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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