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O25867 (TRPC_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:trpC
Ordered Locus Names:HP_1279
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length452 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.

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 – 452452Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154280

Regions

Region1 – 253253Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region254 – 448195N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
O25867 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E5451CE56B75145E

FASTA45250,858
        10         20         30         40         50         60 
MPSVLENILK DKLLEVSDLK KNHALPININ PSDRDFKKAL LEKKTSFILE CKKASPSKGL 

        70         80         90        100        110        120 
IRKDFDLLKI TKTYEKFASC ISVLADSKYF LGSYENIKIV SQHSTKPILC KDFIIDAFQI 

       130        140        150        160        170        180 
KLARMMGANA VLLMLSVLDD KNYLELFNLA KSLNMSVLTE VSNQQEIEHL LKLQYDIIGI 

       190        200        210        220        230        240 
NNRDLHTLKT DINHTLKLRP LLPKDALIIS ESGIYSHAQI KALAPYVNGF LVGSSLMKEK 

       250        260        270        280        290        300 
DLKKACIKLI LGENKVCGLT RIKDAKAVYK NHFIYGGLIF EKSSPRYIKP KEALKITKAV 

       310        320        330        340        350        360 
KKLDFVGVFV KDSIKKIQKI VKKLDLKAVQ LYGYSQKEIA QLKKALPKTC AIWQVISVMS 

       370        380        390        400        410        420 
AKDLVPKTKE ASLILYDTKG DKMGGNGVSF DWEILENVKT PFMLAGGLNL DNIQKALKVE 

       430        440        450 
ALGLDFNSGL EISPGIKNKD KIKRLARILR EY

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000511 Genomic DNA. Translation: AAD08324.1.
PIRG64679.
RefSeqNP_208071.1. NC_000915.1.
YP_006935200.1. NC_018939.1.

3D structure databases

ProteinModelPortalO25867.
SMRO25867. Positions 1-256.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-181675.
STRING85962.HP1279.

Proteomic databases

PRIDEO25867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD08324; AAD08324; HP_1279.
GeneID13870487.
898793.
KEGGheo:C694_06610.
hpy:HP1279.
PATRIC20593935. VBIHelPyl33062_1338.

Phylogenomic databases

eggNOGCOG0134.
KOK13498.
OMAYILECKK.
ProtClustDBPRK09427.

Enzyme and pathway databases

UniPathwayUPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

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

Entry information

Entry nameTRPC_HELPY
AccessionPrimary (citable) accession number: O25867
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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