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Q9KST5 (TRPC_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

  1. Indole-3-glycerol phosphate synthase
    Short name=IGPS
    EC=4.1.1.48
  2. N-(5'-phospho-ribosyl)anthranilate isomerase
    Short name=PRAI
    EC=5.3.1.24
Gene names
Name:trpCF
Ordered Locus Names:VC_1171
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
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 By similarity. HAMAP-Rule MF_00134_B

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00134_B

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00134_B

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.

Subunit structure

Monomer.

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 – 469469Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154285

Regions

Region1 – 271271Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region272 – 469198N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
Q9KST5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AAFF776A0D8EC66E

FASTA46952,038
        10         20         30         40         50         60 
MSEQLSEHIS VQTAQMAQVL VKIVNDKYQW IEERKAKQPL ASFHPLLTRS ERDFYQALSG 

        70         80         90        100        110        120 
DNTVFILECK KASPSKGLIR EEFDLDYIAS VYGEYASAIS VLTDEKYFQG RFEFLPQVRA 

       130        140        150        160        170        180 
QVAQPVLCKD FMVDPYQVYL ARHYQADAIL LMLSVLNDDQ YRELAAVAHD LGMGVLTEVS 

       190        200        210        220        230        240 
NEQELKRAVD LQAKVIGINN RNLRDLTTDL NRTKQLAPLI PQGTIIISES GIYTHQQVRD 

       250        260        270        280        290        300 
LAEFANGFLI GSSLMAQSNL ELAVRKIVLG EHKVCGLTHP DDAVKAYQAG SVFGGLIFVE 

       310        320        330        340        350        360 
KSKRFVDVEQ ARLTMSGAPL QYVGVFQNHP AAQVADIATK LGLFAVQLHG EEDSAYVSEL 

       370        380        390        400        410        420 
RASLPESIEI WKAYGVSDAL PELLPEHIDR HLLDAKVGEQ SGGTGRSFDW RLLPKHSDLM 

       430        440        450        460 
LAGGLSAENV AQAAQLGCRG LDFNSGVESA PGKKDANQLQ QVFQQLRNY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF94330.1.
PIRF82232.
RefSeqNP_230816.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KST5.
SMRQ9KST5. Positions 16-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC1171.

Protocols and materials databases

DNASU2614604.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94330; AAF94330; VC_1171.
GeneID2614604.
KEGGvch:VC1171.
PATRIC20081434. VBIVibCho83274_1120.

Phylogenomic databases

eggNOGCOG0134.
KOK13498.
OMASFILECK.
OrthoDBEOG6WT8JX.
ProtClustDBPRK09427.

Enzyme and pathway databases

BioCycVCHO:VC1171-MONOMER.
UniPathwayUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 2 hits.
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPC_VIBCH
AccessionPrimary (citable) accession number: Q9KST5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways