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Q5XQP9 (TRPF_SACK1) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 42. 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:
N-(5'-phosphoribosyl)anthranilate isomerase

Short name=PRAI
EC=5.3.1.24
Gene names
Name:TRP1
OrganismSaccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889) (Yeast) [Complete proteome]
Taxonomic identifier226230 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00135

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00135

Sequence similarities

Belongs to the TrpF family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtryptophan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionphosphoribosylanthranilate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 226226N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_0000154336

Sequences

Sequence LengthMass (Da)Tools
Q5XQP9 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 79E79FF6030BF5AC

FASTA22624,791
        10         20         30         40         50         60 
MSFVNIRSSR GPVVKVCGLQ SLKAAQCALD SDADLLGIIC VPGRERTVDP VVAMEISALV 

        70         80         90        100        110        120 
RACRTSMSTP KYLVGVFRNQ SKEDVLRIAN DYGIDIVQLH GDEPWQEYQK FLGLPVIKRL 

       130        140        150        160        170        180 
VFPRDCDILL STPSEKTHLF MPLFDSEAGG TGELLDWNSI SDWFAEQGNP ECLQFMLAGG 

       190        200        210        220 
LTPENVSDAL QLHGVIGVDV SGGVETNGMK DMDKITNFVR NAKKES 

« Hide

References

« Hide 'large scale' references
[1]"Parallel inactivation of multiple GAL pathway genes and ecological diversification in yeasts."
Hittinger C.T., Rokas A., Carroll S.B.
Proc. Natl. Acad. Sci. U.S.A. 101:14144-14149(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889.
[2]"Finding functional features in Saccharomyces genomes by phylogenetic footprinting."
Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.
Science 301:71-76(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889.
[3]"The awesome power of yeast evolutionary genetics: New genome sequences and strain resources for the Saccharomyces sensu stricto genus."
Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B., Rine J., Johnston M., Hittinger C.T.
G3 (Bethesda) 1:11-25(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY740027 Genomic DNA. Translation: AAU43745.1.
AACI03000993 Genomic DNA. Translation: EJT43161.1.

3D structure databases

ProteinModelPortalQ5XQP9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG76MKM7.

Enzyme and pathway databases

UniPathwayUPA00035; UER00042.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRPF_SACK1
AccessionPrimary (citable) accession number: Q5XQP9
Secondary accession number(s): J5RY70
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways