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A6L7N0 (TRPF_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:BVU_4092
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length205 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 – 205205N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135
PRO_1000197083

Sequences

Sequence LengthMass (Da)Tools
A6L7N0 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 0FC3766DA0632840

FASTA20522,897
        10         20         30         40         50         60 
MIIKVCGMRE PENIRAIEQA GADWMGFIFF PQSARYVSHR PEYLPEQCHR IGVFVNESSE 

        70         80         90        100        110        120 
NILLKAQEFG LHHIQLHGRE TPEQCRKLKA AGLGVIKVFS IAQESDLQSA GCYEGVCDYF 

       130        140        150        160        170        180 
LFDTACSGYG GSGKTFNWNI LQAYRGKTPF LLSGGLRPGS LSLLLQFKHE QWAGIDLNSG 

       190        200 
FETAPALKDD AAVHTFINQL KQKIQ 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR41694.1.
RefSeqYP_001301316.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L7N0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435590.BVU_4092.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR41694; ABR41694; BVU_4092.
GeneID5305051.
KEGGbvu:BVU_4092.
PATRIC21073284. VBIBacVul85104_4203.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0135.
HOGENOMHOG000161598.
KOK01817.
OMASWNKETY.
OrthoDBEOG6N94DF.
ProtClustDBCLSK822228.

Enzyme and pathway databases

BioCycBVUL435590:GH96-4082-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_BACV8
AccessionPrimary (citable) accession number: A6L7N0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 48 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