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P42391 (TRPB_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. 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:
Tryptophan synthase beta chain

EC=4.2.1.20
Gene names
Name:trpB
Ordered Locus Names:BUsg_267
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine By similarity. HAMAP-Rule MF_00133

Catalytic activity

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O. HAMAP-Rule MF_00133

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00133

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule MF_00133

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Sequence similarities

Belongs to the TrpB family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functiontryptophan synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Tryptophan synthase beta chain HAMAP-Rule MF_00133
PRO_0000098927

Amino acid modifications

Modified residue861N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P42391 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DEBFD45D2C859C30

FASTA39944,247
        10         20         30         40         50         60 
MTLLNPYFGK FGGMYVPQIL MPALYQLEKN FVDAKKDSNF QKSFFNYLKN YAGRPTPLTL 

        70         80         90        100        110        120 
CNNLTNGTKT RIYLKREDLL HGGAHKTNQV LGQAMLAVKM KKKEIIAETG AGQHGVAAAI 

       130        140        150        160        170        180 
ASALFNLKCK IYMGYKDIKR QSPNVFRMKL MGAEVVSVES GSGTLKDACN EALRDWSRNY 

       190        200        210        220        230        240 
QKSHYMIGTA AGPHPYPTIV KEFQKMIGEE AKKQILEQEN RLPDAIIACV GGGSNAIGIF 

       250        260        270        280        290        300 
SDFIDEDVNL IGVEPAGQGI ETGKHGAPLN HGRTGIYFGM KSHLMQSQEG QIEKSWSISA 

       310        320        330        340        350        360 
GLDFPSVGPE HSWLNSIHRA KYVSITDIEA LEAFQILSKK EGIIPALESS HALAYALKLM 

       370        380        390 
YLDPKKEQVF IVNLSGRGDK DIFTVREILK KTEKKHESL 

« 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: CAA79500.1.
AE013218 Genomic DNA. Translation: AAM67825.1.
PIRC49897.
RefSeqNP_660614.1. NC_004061.1.

3D structure databases

ProteinModelPortalP42391.
SMRP42391. Positions 2-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg267.

Proteomic databases

PRIDEP42391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67825; AAM67825; BUsg_267.
GeneID1005469.
KEGGbas:BUsg267.
PATRIC21247339. VBIBucAph100086_0279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0133.
KOK01696.
OMAIGRAEYV.
OrthoDBEOG6GFGH7.
ProtClustDBPRK04346.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-281-MONOMER.
UniPathwayUPA00035; UER00044.

Family and domain databases

HAMAPMF_00133. Trp_synth_beta.
InterProIPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
IPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
[Graphical view]
PANTHERPTHR10314:SF3. PTHR10314:SF3. 1 hit.
PfamPF00291. PALP. 1 hit.
[Graphical view]
PIRSFPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00263. trpB. 1 hit.
PROSITEPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPB_BUCAP
AccessionPrimary (citable) accession number: P42391
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 98 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