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Q8ZEG8 (TRPC_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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:YPO2205, y2049, YP_2003
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length475 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 By similarity. HAMAP-Rule MF_00134_B

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 – 475475Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154287

Regions

Region1 – 279279Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region280 – 475196N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

Sequence LengthMass (Da)Tools
Q8ZEG8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 181CF84E2F15F2FB

FASTA47552,117
        10         20         30         40         50         60 
MQETGGYKTE GYNVGSDKVD SDKTKTVLHQ IVHDKEIWVA ARKLQQPLTR FQNEITQSQR 

        70         80         90        100        110        120 
DFYHALQGDK TVFILECKKA SPSKGVIRDN FNPAEIAGVY KHYASAISVL TDEKYFQGSF 

       130        140        150        160        170        180 
DFLPQVSAAV TQPVLCKDFI IDAYQIQLAR FYHADAILLM LSVLDDEAYR QLAAVAHSLN 

       190        200        210        220        230        240 
MGVLTEASNA EELERAITLG AKVVGINNRD LRDLSIDLNR TRELAPRLPE GVTIISESGI 

       250        260        270        280        290        300 
SHYRQVRELS QFANGFLIGS ALMSEPDLNA AVRRVLLGEN KVCGLTRAQD AATAYHAGAV 

       310        320        330        340        350        360 
YGGLIFVDSS PRYVDIASAR TVISGAPLKY VGVFRHAEIE TVRQTAEQLS LAAVQLHGHE 

       370        380        390        400        410        420 
DQQYINQLRK VLPADCQIWK ALSVGDTMPE RNLQQVERYV LDHGTGGTGQ RFDWSLLADQ 

       430        440        450        460        470 
ALDNVLLAGG LGPDNCDVAA QLGCAGLDVN SGVESAPGIK DPQRIAAVFQ ALRVY 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL20834.1.
AE009952 Genomic DNA. Translation: AAM85614.1.
AE017042 Genomic DNA. Translation: AAS62219.1.
PIRAG0268.
RefSeqNP_669363.1. NC_004088.1.
NP_993342.1. NC_005810.1.
YP_002347176.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZEG8.
SMRQ8ZEG8. Positions 25-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8ZEG8. 2 interactions.
STRING214092.YPO2205.

Proteomic databases

PRIDEQ8ZEG8.

Protocols and materials databases

DNASU1146996.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM85614; AAM85614; y2049.
AAS62219; AAS62219; YP_2003.
GeneID1146996.
1175038.
2765813.
KEGGype:YPO2205.
ypk:y2049.
ypm:YP_2003.

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280458.
KOK13498.
OMASFILECK.
OrthoDBEOG6WT8JX.
ProtClustDBPRK09427.

Enzyme and pathway databases

BioCycYPES214092:GKDD-2174-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_YERPE
AccessionPrimary (citable) accession number: Q8ZEG8
Secondary accession number(s): Q0WEW2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 88 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