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Q9ZJU8 (TRPC_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. 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:trpC
Ordered Locus Names:jhp_1200
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

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_0000154281

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
Q9ZJU8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 153AD3B136C632F0

FASTA45250,678
        10         20         30         40         50         60 
MPSVLENILK DKLLEVAVLK KNHALPINIA PSDRDFKKAL LEKKTSFILE YKKASPSKGL 

        70         80         90        100        110        120 
IRKDFDLLEI TKTYEKFASC VSVLADSKYF LGSYENIKIV SQHSTKPILC KDFIIDAFQI 

       130        140        150        160        170        180 
KLARVMGSNA VLLMLSVLDD KNYLELFNLA KSLNMSVLTE VSNQQEIERL LKLQYDIIGI 

       190        200        210        220        230        240 
NNRDLHTLKT DIFHTLELRP LLPKDAIIIS ESGIYSHAQI KALAPCVNGF LVGSSLMKEK 

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

       310        320        330        340        350        360 
KKLDFVGVFV KDKIKKIAKI AKKLDLKAVQ LYGYSQKEIA QLKKSLPKTC AIWQVVSVAD 

       370        380        390        400        410        420 
SKDLAPKTKE ASLILYDTKG DKMGGNGVSF DWEILENAKT PFMLAGGLNL DNIQKALKIK 

       430        440        450 
ALGLDFNSGL EISPGIKNKD KIKQLARILR EY 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06779.1.
PIRD71836.
RefSeqNP_223918.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZJU8.
SMRQ9ZJU8. Positions 1-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp1200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06779; AAD06779; jhp_1200.
GeneID890448.
KEGGhpj:jhp1200.
PATRIC20607240. VBIHelPyl98156_1301.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0134.
KOK13498.
OMAEKYFQGD.
OrthoDBEOG6WT8JX.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-1236-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZJU8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 89 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