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A4YJI7 (TRPF_BRASO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:BRADO0092
OrganismBradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]
Taxonomic identifier114615 [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_1000018584

Sequences

Sequence LengthMass (Da)Tools
A4YJI7 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 1477358230805F6D

FASTA21923,351
        10         20         30         40         50         60 
MSLLVKICGL TTPETLDAAL DAGAEMVGFV FFPPSPRHVG LTAARELGQQ AKGRALKVAL 

        70         80         90        100        110        120 
TVDADDATFE NIVETLRPDL LQLHGRESIA RIRDLKQRFG LPVMKAVAVA TSADLAPLAG 

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

       190        200        210 
RAGGVDVSSG VERTPGVKDC DMIRNFIRAA RAAEELSVQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU234118 Genomic DNA. Translation: CAL74063.1.
RefSeqYP_001202313.1. NC_009445.1.

3D structure databases

ProteinModelPortalA4YJI7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING114615.BRADO0092.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL74063; CAL74063; BRADO0092.
GeneID5117872.
KEGGbra:BRADO0092.
PATRIC21216514. VBIBraSp122330_0095.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0135.
HOGENOMHOG000161598.
KOK01817.
OMAFVNASRC.
OrthoDBEOG6N94DF.
ProtClustDBPRK01222.

Enzyme and pathway databases

BioCycBSP114615:GJN5-90-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_BRASO
AccessionPrimary (citable) accession number: A4YJI7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 41 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