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P00929 (TRPA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 139. 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·Interactions·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:STM1727
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length268 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 + D-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.

Sequence similarities

Belongs to the TrpA family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

trpBP0A2K122EBI-1028423,EBI-1028431

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268Tryptophan synthase alpha chain HAMAP-Rule MF_00131
PRO_0000098839

Sites

Active site491Proton acceptor
Active site601Proton acceptor

Secondary structure

.................................................... 268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00929 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F409BF1A931581B5

FASTA26828,671
        10         20         30         40         50         60 
MERYENLFAQ LNDRREGAFV PFVTLGDPGI EQSLKIIDTL IDAGADALEL GVPFSDPLAD 

        70         80         90        100        110        120 
GPTIQNANLR AFAAGVTPAQ CFEMLALIRE KHPTIPIGLL MYANLVFNNG IDAFYARCEQ 

       130        140        150        160        170        180 
VGVDSVLVAD VPVEESAPFR QAALRHNIAP IFICPPNADD DLLRQVASYG RGYTYLLSRS 

       190        200        210        220        230        240 
GVTGAENRGA LPLHHLIEKL KEYHAAPALQ GFGISSPEQV SAAVRAGAAG AISGSAIVKI 

       250        260 
IEKNLASPKQ MLAELRSFVS AMKAASRA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison."
Nichols B.P., Yanofsky C.
Proc. Natl. Acad. Sci. U.S.A. 76:5244-5248(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides."
Schneider W.P., Nichols B.P., Yanofsky C.
Proc. Natl. Acad. Sci. U.S.A. 78:2169-2173(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[4]"Amino acid sequence studies with the tryptophan synthetase alpha chain of Salmonella typhimurium."
Li S.-L., Yanofsky C.
J. Biol. Chem. 248:1830-1836(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[5]"Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium."
Hyde C.C., Ahmed S.A., Padlan E.A., Miles E.W., Davies D.R.
J. Biol. Chem. 263:17857-17871(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[6]"Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes."
Rhee S., Parris K.D., Hyde C.C., Ahmed S.A., Miles E.W., Davies D.R.
Biochemistry 36:7664-7680(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]"Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49."
Rhee S., Miles E.W., Davies D.R.
J. Biol. Chem. 273:8553-8555(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[8]"Refined structure of the native form of the tryptophan synthase multienzyme complex from Salmonella typhimurium."
Hyde C.C., Parris K.D., Bhat T.N., Brown C., Ahmed S.A., Miles E.W., Davies D.R.
Submitted (JUL-1998) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[9]"Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase."
Sachpatzidis A., Dealwis C., Lubetsky J.B., Liang P.-H., Anderson K.S., Lolis E.
Biochemistry 38:12665-12674(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[10]"Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase."
Weyand M., Schlichting I.
J. Biol. Chem. 275:41058-41063(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[11]"On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase."
Kulik V., Weyand M., Seidel R., Niks D., Arac D., Dunn M.F., Schlichting I.
J. Mol. Biol. 324:677-690(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 17-268.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01376 Genomic DNA. Translation: CAA24666.1.
J01810 Genomic DNA. Translation: AAA27235.1.
AE006468 Genomic DNA. Translation: AAL20645.1.
PIRTSEBAT. A93837.
RefSeqNP_460686.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A50X-ray2.30A1-268[»]
1A5AX-ray1.90A1-268[»]
1A5BX-ray2.00A1-268[»]
1A5SX-ray2.30A1-268[»]
1BEUX-ray1.90A1-268[»]
1BKSX-ray2.20A1-268[»]
1C29X-ray2.30A1-268[»]
1C8VX-ray2.20A1-268[»]
1C9DX-ray2.30A1-268[»]
1CW2X-ray2.00A1-268[»]
1CX9X-ray2.30A1-268[»]
1FUYX-ray2.25A1-268[»]
1K3UX-ray1.70A1-268[»]
1K7EX-ray2.30A1-268[»]
1K7FX-ray1.90A1-268[»]
1K7XX-ray1.70A1-268[»]
1K8XX-ray1.90A1-268[»]
1K8YX-ray1.50A1-268[»]
1K8ZX-ray1.70A1-268[»]
1KFBX-ray1.90A1-268[»]
1KFCX-ray1.50A1-268[»]
1KFEX-ray1.75A1-268[»]
1KFJX-ray1.80A1-268[»]
1KFKX-ray2.40A1-268[»]
1QOPX-ray1.40A1-268[»]
1QOQX-ray1.80A1-268[»]
1TJPX-ray1.50A1-268[»]
1TTPX-ray2.30A1-268[»]
1TTQX-ray2.00A1-268[»]
1UBSX-ray1.90A1-268[»]
1WBJX-ray1.50A1-268[»]
2CLEX-ray1.50A1-268[»]
2CLFX-ray1.70A1-268[»]
2CLHX-ray1.70A1-268[»]
2CLIX-ray1.70A1-268[»]
2CLKX-ray1.50A1-268[»]
2CLLX-ray1.60A1-268[»]
2CLMX-ray1.51A1-268[»]
2CLOX-ray1.50A1-268[»]
2J9XX-ray1.90A1-268[»]
2J9YX-ray1.80A1-268[»]
2J9ZX-ray1.80A1-268[»]
2RH9X-ray1.70A1-268[»]
2RHGX-ray2.00A1-268[»]
2TRSX-ray2.04A1-268[»]
2TSYX-ray2.50A1-268[»]
2TYSX-ray1.90A1-268[»]
2WSYX-ray3.05A1-268[»]
3CEPX-ray2.10A1-268[»]
3PR2X-ray1.85A2-267[»]
4HN4X-ray1.64A1-268[»]
4HPJX-ray1.45A1-268[»]
4HPXX-ray1.65A1-268[»]
4HT3X-ray1.30A1-268[»]
4KKXX-ray1.77A1-268[»]
ProteinModelPortalP00929.
SMRP00929. Positions 1-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-1033N.
IntActP00929. 1 interaction.
MINTMINT-112862.
STRING99287.STM1727.

Proteomic databases

PRIDEP00929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20645; AAL20645; STM1727.
GeneID1253246.
KEGGstm:STM1727.
PATRIC32381967. VBISalEnt20916_1823.

Phylogenomic databases

HOGENOMHOG000223814.
KOK01695.
OMADYPPEEC.
OrthoDBEOG6RVG0K.
ProtClustDBPRK13111.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1736-MONOMER.
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. SSF51366. 1 hit.
TIGRFAMsTIGR00262. trpA. 1 hit.
PROSITEPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00929.
PROP00929.

Entry information

Entry nameTRPA_SALTY
AccessionPrimary (citable) accession number: P00929
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 139 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