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Q1MND7 (TRPF_RHIL3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:RL0020
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length222 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 – 222222N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_1000018630

Sequences

Sequence LengthMass (Da)Tools
Q1MND7 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 20648D1A6C5BE32B

FASTA22223,903
        10         20         30         40         50         60 
MRPDIKICGL KTPEAVDRAL KRGATHIGFI FFEKSPRYIE PDLAAKLAEP ARGKAKIVAV 

        70         80         90        100        110        120 
VVDPTNDELD EIVSLLKPDM LQLHGNESPE HVLTIKALYG LPVMKVFSVR TADDLKRVEA 

       130        140        150        160        170        180 
YIGIADRFLF DAKAPKGSEL PGGNGISFDW SLLSWLDGSV DYMLSGGLNK DNVAEALFVT 

       190        200        210        220 
KAPGIDVSSG VETAPGVKSV AKIDEFFDAV EKANAPMMAS GS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM236080 Genomic DNA. Translation: CAK05508.1.
RefSeqYP_765624.1. NC_008380.1.

3D structure databases

ProteinModelPortalQ1MND7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216596.RL0020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK05508; CAK05508; RL0020.
GeneID4401915.
KEGGrle:RL0020.
PATRIC23136377. VBIRhiLeg32091_1149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0135.
HOGENOMHOG000161598.
KOK01817.
OMADILQLHG.
OrthoDBEOG6N94DF.

Enzyme and pathway databases

BioCycRLEG216596:GKE5-22-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_RHIL3
AccessionPrimary (citable) accession number: Q1MND7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: May 14, 2014
This is version 50 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