Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2YRR5 (TRPD_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Anthranilate phosphoribosyltransferase

EC=2.4.2.18
Gene names
Name:trpD
Ordered Locus Names:BAB1_1163
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA) By similarity. HAMAP-Rule MF_00211

Catalytic activity

N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00211

Cofactor

Binds 2 magnesium ions per monomer By similarity. HAMAP-Rule MF_00211

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. HAMAP-Rule MF_00211

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00211

Sequence similarities

Belongs to the anthranilate phosphoribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Anthranilate phosphoribosyltransferase HAMAP-Rule MF_00211
PRO_0000227140

Regions

Region84 – 852Phosphoribosylpyrophosphate binding By similarity
Region91 – 944Phosphoribosylpyrophosphate binding By similarity
Region109 – 1179Phosphoribosylpyrophosphate binding By similarity

Sites

Metal binding931Magnesium 1 By similarity
Metal binding2251Magnesium 2 By similarity
Metal binding2261Magnesium 1 By similarity
Metal binding2261Magnesium 2 By similarity
Binding site811Anthranilate 1; via carbonyl oxygen By similarity
Binding site811Phosphoribosylpyrophosphate; via amide nitrogen By similarity
Binding site891Phosphoribosylpyrophosphate By similarity
Binding site1121Anthranilate 1 By similarity
Binding site1211Phosphoribosylpyrophosphate; via amide nitrogen By similarity
Binding site1671Anthranilate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YRR5 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 182891532AE4FCDA

FASTA33934,839
        10         20         30         40         50         60 
MADLKPYIAK AASGEPLPLG DAKAAFDIMM SGQATPSQIG GFLMALRVRG ETVPEIAGAV 

        70         80         90        100        110        120 
ASMRSRMIPV IAPDDAMDIV GTGGDQSGSY NVSSCTAFVV AGAGVPVAKH GNRALSSRSG 

       130        140        150        160        170        180 
AADALAALGI NIEADADTIG RSISEAGLGF MFAPMHHSAM RHVGPSRVEL GTRTIFNLLG 

       190        200        210        220        230        240 
PLSNPASVKR QLVGVFAPQW LEPLAHVLKE LGSETAWVVY GDGLDEMTTA GTTQVAALEN 

       250        260        270        280        290        300 
GQIRTFEITP EEVGLRRCSP AELKGGEAAE NAKALLGVLE GKDSAYRDIV LLNSGAALVV 

       310        320        330 
AGKAENLKDG IAQAVQSIDS GAALAVLQKV IAVSNDKPA 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ11119.1.
RefSeqYP_414554.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YRR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_1163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ11119; CAJ11119; BAB1_1163.
GeneID3787802.
KEGGbmf:BAB1_1163.
PATRIC17845281. VBIBruMel86222_1210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0547.
HOGENOMHOG000230451.
KOK00766.
OMAQPFPRPD.
OrthoDBEOG6D5G6B.

Enzyme and pathway databases

BioCycBABO359391:GKDV-1185-MONOMER.
BMEL359391:GJOQ-1185-MONOMER.
UniPathwayUPA00035; UER00041.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
HAMAPMF_00211. TrpD.
InterProIPR005940. Anthranilate_Pribosyl_Tfrase.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
[Graphical view]
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
TIGRFAMsTIGR01245. trpD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRPD_BRUA2
AccessionPrimary (citable) accession number: Q2YRR5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 54 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

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names