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Q8U093 (TRPB1_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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 1

EC=4.2.1.20
Gene names
Name:trpB1
Ordered Locus Names:PF1706
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Tryptophan synthase beta chain 1 HAMAP-Rule MF_00133
PRO_0000099050

Amino acid modifications

Modified residue821N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

.............................................................. 388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8U093 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 62C811579520E04B

FASTA38842,529
        10         20         30         40         50         60 
MWFGEFGGQY VPETLIEPLK ELEKAYKRFK DDEEFNRQLN YYLKTWAGRP TPLYYAKRLT 

        70         80         90        100        110        120 
EKIGGAKIYL KREDLVHGGA HKTNNAIGQA LLAKFMGKTR LIAETGAGQH GVATAMAGAL 

       130        140        150        160        170        180 
LGMKVDIYMG AEDVERQKMN VFRMKLLGAN VIPVNSGSRT LKDAINEALR DWVATFEYTH 

       190        200        210        220        230        240 
YLIGSVVGPH PYPTIVRDFQ SVIGREAKAQ ILEAEGQLPD VIVACVGGGS NAMGIFYPFV 

       250        260        270        280        290        300 
NDKKVKLVGV EAGGKGLESG KHSASLNAGQ VGVFHGMLSY FLQDEEGQIK PTHSIAPGLD 

       310        320        330        340        350        360 
YPGVGPEHAY LKKIQRAEYV TVTDEEALKA FHELSRTEGI IPALESAHAV AYAMKLAKEM 

       370        380 
SRDEIIIVNL SGRGDKDLDI VLKVSGNV 

« Hide

References

« Hide 'large scale' references
[1]"Overexpression in Escherichia coli of the AT-rich trpA and trpB genes from the hyperthermophilic archaeon Pyrococcus furiosus."
Ishida M., Oshima T., Yutani K.
FEMS Microbiol. Lett. 216:179-183(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB080770 Genomic DNA. Translation: BAC11855.1.
AE009950 Genomic DNA. Translation: AAL81830.1.
RefSeqNP_579435.1. NC_003413.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V8ZX-ray2.21A/B/C/D1-388[»]
1WDWX-ray3.00B/D/F/H/J/L1-385[»]
ProteinModelPortalQ8U093.
SMRQ8U093. Positions 1-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1706.

Proteomic databases

PRIDEQ8U093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81830; AAL81830; PF1706.
GeneID1469583.
KEGGpfu:PF1706.

Phylogenomic databases

eggNOGCOG0133.
HOGENOMHOG000161710.
KOK01696.
OMAVHTLMNV.

Enzyme and pathway databases

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]
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...

Other

EvolutionaryTraceQ8U093.

Entry information

Entry nameTRPB1_PYRFU
AccessionPrimary (citable) accession number: Q8U093
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 85 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways