Tryptophan synthase alpha chain

Details

Name
Tryptophan synthase alpha chain
Synonyms
  • 4.2.1.20
Gene Name
trpA
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0017318|Tryptophan synthase alpha chain
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLAD
GPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQ
VGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDDLLRQVASYGRGYTYLLSRS
GVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASRA
Number of residues
268
Molecular Weight
28670.485
Theoretical pI
5.34
GO Classification
Functions
tryptophan synthase activity
General Function
Tryptophan synthase activity
Specific Function
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0017319|Tryptophan synthase alpha chain (trpA)
ATGGAACGCTACGAAAATTTATTTGCCCAACTCAACGATCGCCGGGAAGGCGCTTTTGTC
CCCTTCGTGACCCTGGGCGACCCTGGCATTGAACAGTCACTGAAAATTATTGACACACTG
ATTGACGCTGGCGCCGACGCTCTGGAACTGGGGGTTCCCTTCTCCGATCCGCTGGCCGAT
GGCCCTACCATCCAGAATGCGAACTTACGCGCCTTCGCCGCTGGCGTCACGCCGGCTCAG
TGTTTTGAAATGCTGGCGCTGATTCGTGAAAAACACCCGACCATTCCGATTGGCCTGCTA
ATGTACGCGAATCTGGTGTTCAATAACGGCATAGATGCGTTCTATGCCCGTTGTGAACAG
GTTGGCGTAGATTCCGTGCTGGTCGCAGATGTCCCGGTTGAAGAATCGGCCCCCTTCCGC
CAGGCAGCGTTACGGCATAATATCGCGCCGATCTTCATCTGCCCGCCAAATGCGGATGAC
GATCTTCTGCGCCAGGTCGCATCTTACGGCCGCGGTTACACCTACCTGCTTTCGCGTTCG
GGTGTCACCGGCGCGGAAAACCGTGGCGCATTGCCGTTGCATCATCTCATTGAGAAGCTT
AAAGAGTACCATGCCGCGCCTGCGTTACAGGGCTTCGGTATCTCCTCGCCGGAACAGGTG
TCTGCGGCCGTGCGTGCCGGGGCGGCTGGCGCTATCTCCGGCTCAGCCATTGTCAAGATT
ATCGAGAAAAACCTCGCGTCTCCCAAACAGATGTTGGCGGAGCTCAGGTCCTTTGTCTCA
GCCATGAAAGCCGCCAGCCGCGCATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00929
UniProtKB Entry NameTRPA_SALTY
GenBank Protein ID47939
GenBank Gene IDV01376
General References
  1. Nichols BP, Yanofsky C: Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5244-8. [PubMed:388433]
  2. Schneider WP, Nichols BP, Yanofsky C: Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2169-73. [PubMed:7017727]
  3. McClelland M, Sanderson KE, Spieth J, Clifton SW, 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, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [PubMed:11677609]
  4. Li SL, Yanofsky C: Amino acid sequence studies with the tryptophan synthetase chain of Salmonella typhimurium. J Biol Chem. 1973 Mar 10;248(5):1830-6. [PubMed:4571777]
  5. Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR: Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J Biol Chem. 1988 Nov 25;263(33):17857-71. [PubMed:3053720]
  6. Rhee S, Parris KD, Hyde CC, Ahmed SA, Miles EW, Davies DR: 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. Biochemistry. 1997 Jun 24;36(25):7664-80. [PubMed:9201907]
  7. Rhee S, Miles EW, Davies DR: 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. J Biol Chem. 1998 Apr 10;273(15):8553-5. [PubMed:9535826]
  8. Sachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E: Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase. Biochemistry. 1999 Sep 28;38(39):12665-74. [PubMed:10504236]
  9. Weyand M, Schlichting I: Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase. J Biol Chem. 2000 Dec 29;275(52):41058-63. [PubMed:11034989]
  10. Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I: On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase. J Mol Biol. 2002 Dec 6;324(4):677-90. [PubMed:12460570]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB077322-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATEexperimentalunknownDetails
DB077452-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATEexperimentalunknownDetails
DB077482-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATEexperimentalunknownDetails
DB077735-FLUOROINDOLE PROPANOL PHOSPHATEexperimentalunknownDetails
DB078904-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACIDexperimentalunknownDetails
DB078944-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACIDexperimentalunknownDetails
DB079254-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACIDexperimentalunknownDetails
DB07951N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACIDexperimentalunknownDetails
DB07952N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACIDexperimentalunknownDetails
DB07953N-[1H-INDOL-3-YL-ACETYL]VALINE ACIDexperimentalunknownDetails
DB04143Indole-3-Glycerol PhosphateexperimentalunknownDetails
DB03171Indole-3-Propanol PhosphateexperimentalunknownDetails