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B2SVN9 (TRPF_XANOP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:PXO_01268
OrganismXanthomonas oryzae pv. oryzae (strain PXO99A) [Complete proteome] [HAMAP]
Taxonomic identifier360094 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

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_1000095951

Sequences

Sequence LengthMass (Da)Tools
B2SVN9 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 88A84C88D7D967AE

FASTA22224,118
        10         20         30         40         50         60 
MNRSLYRTRI KFCGMTRAGD IRLAGELGVD AVGFIFAHGS PRRVAPAEAR AMRQATAPMV 

        70         80         90        100        110        120 
DVVALFRNNS KEEVREVVRT VRPTLLQFHG EEEDAFCRSF NLPYLKAVPM GSTGVNGEDA 

       130        140        150        160        170        180 
NARTLQLSYP NTAGFLFDSH APGAGGGTGK TFDWSRLPTG LHRPFLLAGG INAGNVFDAI 

       190        200        210        220 
VATLPWGVDV SSGVELAPGI KDGHKMRKFV EEVRRADCHE MS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000967 Genomic DNA. Translation: ACD60113.1.
RefSeqYP_001914645.1. NC_010717.1.

3D structure databases

ProteinModelPortalB2SVN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360094.PXO_01268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD60113; ACD60113; PXO_01268.
GeneID6307049.
KEGGxop:PXO_01268.
PATRIC24126550. VBIXanOry73153_3626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0135.
HOGENOMHOG000161598.
KOK01817.
OMASKPWWLA.
OrthoDBEOG6N94DF.

Enzyme and pathway databases

BioCycXORY360094:GI45-3530-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_XANOP
AccessionPrimary (citable) accession number: B2SVN9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 40 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