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P42392 (TRPD_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. 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:BUsg_269
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length335 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 – 335335Anthranilate phosphoribosyltransferase HAMAP-Rule MF_00211
PRO_0000154435

Regions

Region82 – 832Phosphoribosylpyrophosphate binding By similarity
Region89 – 924Phosphoribosylpyrophosphate binding By similarity
Region107 – 1159Phosphoribosylpyrophosphate binding By similarity

Sites

Metal binding911Magnesium 1 By similarity
Metal binding2231Magnesium 2 By similarity
Metal binding2241Magnesium 1 By similarity
Metal binding2241Magnesium 2 By similarity
Binding site791Anthranilate 1; via carbonyl oxygen By similarity
Binding site791Phosphoribosylpyrophosphate; via amide nitrogen By similarity
Binding site871Phosphoribosylpyrophosphate By similarity
Binding site1101Anthranilate 1 By similarity
Binding site1191Phosphoribosylpyrophosphate; via amide nitrogen By similarity
Binding site1651Anthranilate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P42392 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E33F51F2126013AD

FASTA33538,090
        10         20         30         40         50         60 
MQNIFNKIYE SKSLNQEESY QLFKSIALGK INEIQLSSIL TAMQMHGESE KEILGAIYAF 

        70         80         90        100        110        120 
SERMKFFPRP NYIFSDIVGT GGDSKNTINV STSSAFVAAS CGFKIIKHCN KGVSSKSGSS 

       130        140        150        160        170        180 
DLLNKFKINL NTSLENSKKI LDKLNICFLF APKYHSVFKY ASKTRSILKI KTIFNLLGPF 

       190        200        210        220        230        240 
LNPSRPPLTL IGVYKKDLVN PMSRILKKLK YQRGIILHGD DTDEVTLHGT TYISELLNNK 

       250        260        270        280        290        300 
IYSYELEPED FGIKRHSKSI FVEYSPEENY HIIKKTMQGK GEKLHEELIA VNVALLLKIF 

       310        320        330 
GHENLKENTK IALKKIRSGD VYKHIMQVSN MLKED 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequence of a putative trpDC(F)BA operon in Buchnera aphidicola (endosymbiont of the aphid Schizaphis graminum)."
Munson M.A., Baumann P.
J. Bacteriol. 175:6426-6432(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z19055 Genomic DNA. Translation: CAA79498.1.
AE013218 Genomic DNA. Translation: AAM67827.1.
PIRA49897.
RefSeqNP_660616.1. NC_004061.1.

3D structure databases

ProteinModelPortalP42392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67827; AAM67827; BUsg_269.
GeneID1005471.
KEGGbas:BUsg269.
PATRIC21247343. VBIBucAph100086_0281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0547.
KOK00766.
OMAQPFPRPD.
OrthoDBEOG6D5G6B.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-283-MONOMER.
UniPathwayUPA00035; UER00041.

Family and domain databases

Gene3D3.40.1030.10. 2 hits.
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_BUCAP
AccessionPrimary (citable) accession number: P42392
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 97 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names