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Q8U094 (TRPA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 alpha chain
EC=4.2.1.20
Gene names
Name:trpA
Ordered Locus Names:PF1705
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. HAMAP-Rule MF_00131

Catalytic activity

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O. HAMAP-Rule MF_00131

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule MF_00131

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Sequence similarities

Belongs to the TrpA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Tryptophan synthase alpha chain HAMAP-Rule MF_00131
PRO_0000098897

Sites

Active site361Proton acceptor
Active site471Proton acceptor

Secondary structure

1 .......................................... 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8U094 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 45D6C877FB8393EE

FASTA24827,497
        10         20         30         40         50         60 
MFKDGSLIPY LTAGDPDKQS TLNFLLALDE YAGAIELGIP FSDPIADGKT IQESHYRALK 

        70         80         90        100        110        120 
NGFKLREAFW IVKEFRRHSS TPIVLMTYYN PIYRAGVRNF LAEAKASGVD GILVVDLPVF 

       130        140        150        160        170        180 
HAKEFTEIAR EEGIKTVFLA APNTPDERLK VIDDMTTGFV YLVSLYGTTG AREEIPKTAY 

       190        200        210        220        230        240 
DLLRRAKRIC RNKVAVGFGV SKREHVVSLL KEGANGVVVG SALVKIIGEK GREATEFLKK 


KVEELLGI

« 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.
[3]"Structures of mutant tryptophan synthase alpha-subunits from a hyperthermophile, Pyrococcus furiosus."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB080770 Genomic DNA. Translation: BAC11856.1.
AE009950 Genomic DNA. Translation: AAL81829.1.
RefSeqNP_579434.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GEQX-ray2.00A/B1-248[»]
1WDWX-ray3.00A/C/E/G/I/K1-248[»]
2DZPX-ray2.40A/B1-248[»]
2DZSX-ray2.40A/B1-248[»]
2DZTX-ray2.40A/B1-248[»]
2DZUX-ray2.46A/B1-248[»]
2DZVX-ray2.40A/B1-248[»]
2DZWX-ray2.40A/B1-248[»]
2DZXX-ray2.40A/B1-248[»]
2E09X-ray2.40A/B1-248[»]
ProteinModelPortalQ8U094.
SMRQ8U094. Positions 1-248.
ModBaseSearch...

Protein-protein interaction databases

STRING186497.PF1705.

Proteomic databases

PRIDEQ8U094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81829; AAL81829; PF1705.
GeneID1469582.
KEGGpfu:PF1705.

Phylogenomic databases

eggNOGCOG0159.
HOGENOMHOG000223815.
KOK01695.
OMAVFICPPN.
ProtClustDBPRK13111.

Enzyme and pathway databases

UniPathwayUPA00035; UER00044.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00131. Trp_synth_alpha.
InterProIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR00262. trpA. 1 hit.
PROSITEPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8U094.

Entry information

Entry nameTRPA_PYRFU
AccessionPrimary (citable) accession number: Q8U094
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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