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A5E8A5 (TRPF_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:trpF
Ordered Locus Names:BBta_0098
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length219 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 – 219219N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_1000018583

Sequences

Sequence LengthMass (Da)Tools
A5E8A5 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 0B6CCC92886B58E2

FASTA21923,234
        10         20         30         40         50         60 
MSLLVKICGL TTPETLGAAL DAGAEMVGFV FFPPSPRHVG LTAARELGQQ AKGRALKVAL 

        70         80         90        100        110        120 
TVDADDATFE NIVETLRPDL LQLHGRESVA RIRDLKQRFG LPVMKAIAVA TTADLVPLAG 

       130        140        150        160        170        180 
YADVCDRILF DARAPKDATR PGGLGATFDW HVLDALALDR PFMVSGGLSA DNVAEAVRIT 

       190        200        210 
RAGGVDVSSG VERAPGVKDC DMIRNFIRAA RAAEELSVQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ32399.1.
RefSeqYP_001236305.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5E8A5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288000.BBta_0098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ32399; ABQ32399; BBta_0098.
GeneID5148919.
KEGGbbt:BBta_0098.
PATRIC21201196. VBIBraSp29847_0303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0135.
HOGENOMHOG000161598.
KOK01817.
OMADILQLHG.
OrthoDBEOG6N94DF.

Enzyme and pathway databases

BioCycBSP288000:GJBR-94-MONOMER.
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_BRASB
AccessionPrimary (citable) accession number: A5E8A5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 42 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