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P00929

- TRPA_SALTY

UniProt

P00929 - TRPA_SALTY

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Protein

Tryptophan synthase alpha chain

Gene

trpA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Proton acceptor
Active sitei60 – 601Proton acceptor

GO - Molecular functioni

  1. tryptophan synthase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1736-MONOMER.
UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase alpha chainUniRule annotation (EC:4.2.1.20UniRule annotation)
Gene namesi
Name:trpAUniRule annotation
Ordered Locus Names:STM1727
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268Tryptophan synthase alpha chainPRO_0000098839Add
BLAST

Proteomic databases

PRIDEiP00929.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.

Binary interactionsi

WithEntry#Exp.IntActNotes
trpBP0A2K122EBI-1028423,EBI-1028431

Protein-protein interaction databases

DIPiDIP-1033N.
IntActiP00929. 1 interaction.
MINTiMINT-112862.
STRINGi99287.STM1727.

Structurei

Secondary structure

1
268
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311
Beta strandi18 – 247
Turni25 – 284
Helixi30 – 4213
Beta strandi46 – 516
Beta strandi58 – 603
Helixi62 – 7312
Helixi78 – 9114
Beta strandi93 – 953
Beta strandi97 – 1015
Helixi103 – 1075
Helixi111 – 12111
Beta strandi125 – 1284
Helixi133 – 1353
Helixi137 – 1459
Beta strandi149 – 1513
Helixi160 – 16910
Beta strandi174 – 1818
Beta strandi185 – 1873
Helixi194 – 2029
Beta strandi208 – 2136
Helixi217 – 2259
Beta strandi229 – 2335
Helixi235 – 2439
Turni244 – 2463
Helixi248 – 26417
Turni265 – 2673

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00929.
SMRiP00929. Positions 1-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00929.

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpA family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000223814.
KOiK01695.
OMAiNSEGYTY.
OrthoDBiEOG6RVG0K.
PhylomeDBiP00929.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00131. Trp_synth_alpha.
InterProiIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamiPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00262. trpA. 1 hit.
PROSITEiPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00929-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERYENLFAQ LNDRREGAFV PFVTLGDPGI EQSLKIIDTL IDAGADALEL
60 70 80 90 100
GVPFSDPLAD GPTIQNANLR AFAAGVTPAQ CFEMLALIRE KHPTIPIGLL
110 120 130 140 150
MYANLVFNNG IDAFYARCEQ VGVDSVLVAD VPVEESAPFR QAALRHNIAP
160 170 180 190 200
IFICPPNADD DLLRQVASYG RGYTYLLSRS GVTGAENRGA LPLHHLIEKL
210 220 230 240 250
KEYHAAPALQ GFGISSPEQV SAAVRAGAAG AISGSAIVKI IEKNLASPKQ
260
MLAELRSFVS AMKAASRA
Length:268
Mass (Da):28,671
Last modified:July 21, 1986 - v1
Checksum:iF409BF1A931581B5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01376 Genomic DNA. Translation: CAA24666.1.
J01810 Genomic DNA. Translation: AAA27235.1.
AE006468 Genomic DNA. Translation: AAL20645.1.
PIRiA93837. TSEBAT.
RefSeqiNP_460686.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20645; AAL20645; STM1727.
GeneIDi1253246.
KEGGistm:STM1727.
PATRICi32381967. VBISalEnt20916_1823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01376 Genomic DNA. Translation: CAA24666.1 .
J01810 Genomic DNA. Translation: AAA27235.1 .
AE006468 Genomic DNA. Translation: AAL20645.1 .
PIRi A93837. TSEBAT.
RefSeqi NP_460686.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A50 X-ray 2.30 A 1-268 [» ]
1A5A X-ray 1.90 A 1-268 [» ]
1A5B X-ray 2.00 A 1-268 [» ]
1A5S X-ray 2.30 A 1-268 [» ]
1BEU X-ray 1.90 A 1-268 [» ]
1BKS X-ray 2.20 A 1-268 [» ]
1C29 X-ray 2.30 A 1-268 [» ]
1C8V X-ray 2.20 A 1-268 [» ]
1C9D X-ray 2.30 A 1-268 [» ]
1CW2 X-ray 2.00 A 1-268 [» ]
1CX9 X-ray 2.30 A 1-268 [» ]
1FUY X-ray 2.25 A 1-268 [» ]
1K3U X-ray 1.70 A 1-268 [» ]
1K7E X-ray 2.30 A 1-268 [» ]
1K7F X-ray 1.90 A 1-268 [» ]
1K7X X-ray 1.70 A 1-268 [» ]
1K8X X-ray 1.90 A 1-268 [» ]
1K8Y X-ray 1.50 A 1-268 [» ]
1K8Z X-ray 1.70 A 1-268 [» ]
1KFB X-ray 1.90 A 1-268 [» ]
1KFC X-ray 1.50 A 1-268 [» ]
1KFE X-ray 1.75 A 1-268 [» ]
1KFJ X-ray 1.80 A 1-268 [» ]
1KFK X-ray 2.40 A 1-268 [» ]
1QOP X-ray 1.40 A 1-268 [» ]
1QOQ X-ray 1.80 A 1-268 [» ]
1TJP X-ray 1.50 A 1-268 [» ]
1TTP X-ray 2.30 A 1-268 [» ]
1TTQ X-ray 2.00 A 1-268 [» ]
1UBS X-ray 1.90 A 1-268 [» ]
1WBJ X-ray 1.50 A 1-268 [» ]
2CLE X-ray 1.50 A 1-268 [» ]
2CLF X-ray 1.70 A 1-268 [» ]
2CLH X-ray 1.70 A 1-268 [» ]
2CLI X-ray 1.70 A 1-268 [» ]
2CLK X-ray 1.50 A 1-268 [» ]
2CLL X-ray 1.60 A 1-268 [» ]
2CLM X-ray 1.51 A 1-268 [» ]
2CLO X-ray 1.50 A 1-268 [» ]
2J9X X-ray 1.90 A 1-268 [» ]
2J9Y X-ray 1.80 A 1-268 [» ]
2J9Z X-ray 1.80 A 1-268 [» ]
2RH9 X-ray 1.70 A 1-268 [» ]
2RHG X-ray 2.00 A 1-268 [» ]
2TRS X-ray 2.04 A 1-268 [» ]
2TSY X-ray 2.50 A 1-268 [» ]
2TYS X-ray 1.90 A 1-268 [» ]
2WSY X-ray 3.05 A 1-268 [» ]
3CEP X-ray 2.10 A 1-268 [» ]
3PR2 X-ray 1.85 A 2-267 [» ]
4HN4 X-ray 1.64 A 1-268 [» ]
4HPJ X-ray 1.45 A 1-268 [» ]
4HPX X-ray 1.65 A 1-268 [» ]
4HT3 X-ray 1.30 A 1-268 [» ]
4KKX X-ray 1.77 A 1-268 [» ]
ProteinModelPortali P00929.
SMRi P00929. Positions 1-268.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-1033N.
IntActi P00929. 1 interaction.
MINTi MINT-112862.
STRINGi 99287.STM1727.

Proteomic databases

PRIDEi P00929.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20645 ; AAL20645 ; STM1727 .
GeneIDi 1253246.
KEGGi stm:STM1727.
PATRICi 32381967. VBISalEnt20916_1823.

Phylogenomic databases

HOGENOMi HOG000223814.
KOi K01695.
OMAi NSEGYTY.
OrthoDBi EOG6RVG0K.
PhylomeDBi P00929.

Enzyme and pathway databases

UniPathwayi UPA00035 ; UER00044 .
BioCyci SENT99287:GCTI-1736-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00929.
PROi P00929.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00131. Trp_synth_alpha.
InterProi IPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view ]
Pfami PF00290. Trp_syntA. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 1 hit.
TIGRFAMsi TIGR00262. trpA. 1 hit.
PROSITEi PS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiTRPA_SALTY
AccessioniPrimary (citable) accession number: P00929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3