Tryptophan synthase beta chain

Details

Name
Tryptophan synthase beta chain
Synonyms
  • 4.2.1.20
Gene Name
trpB
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0012830|Tryptophan synthase beta chain
MTTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALT
KCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASA
LASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGS
YETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGM
FADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSI
SAGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALK
MMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI
Number of residues
397
Molecular Weight
42867.63
Theoretical pI
6.27
GO Classification
Functions
tryptophan synthase activity
General Function
Tryptophan synthase activity
Specific Function
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012831|Tryptophan synthase beta chain (trpB)
ATGACAACACTTCTCAACCCCTACTTTGGTGAATTCGGCGGCATGTATGTGCCGCAGATC
CTGATGCCTGCGCTGAACCAGCTTGAAGAGGCCTTCGTCAGCGCGCAAAAAGATCCTGAA
TTTCAGGCGCAATTCGCCGATCTGCTAAAAAACTACGCGGGACGCCCCACCGCGCTGACG
AAATGCCAGAACATTACCGCCGGTACGCGTACCACGTTGTATTTAAAGCGCGAAGATTTA
CTGCACGGCGGCGCGCACAAAACCAATCAGGTACTGGGTCAGGCGCTGCTGGCCAAACGG
ATGGGTAAAAGCGAGATTATCGCTGAAACCGGCGCCGGTCAGCACGGCGTCGCCTCTGCG
CTCGCCAGCGCCCTGCTGGGTCTGAAATGCCGTATCTATATGGGCGCCAAAGACGTTGAG
CGCCAGTCGCCGAACGTCTTCCGTATGCGTCTGATGGGCGCTGAGGTCATCCCGGTTCAT
AGCGGCTCCGCTACGCTAAAAGATGCCTGTAACGAGGCGCTGCGCGACTGGTCCGGTAGT
TACGAAACCGCGCACTATATGCTCGGCACGGCGGCAGGACCGCATCCCTATCCCACCATC
GTTCGCGAGTTCCAGCGCATGATTGGCGAAGAGACGAAAGCGCAAATCCTCGACAAAGAG
GGCCGTCTGCCAGATGCCGTTATCGCTTGCGTCGGTGGCGGCTCAAACGCTATCGGGATG
TTTGCCGATTTTATTAATGATACCAGCGTCGGGCTAATAGGCGTTGAACCTGGTGGTCAT
GGTATTGAAACCGGCGAGCATGGCGCGCCGCTTAAACATGGTCGCGTTGGCATCTATTTC
GGGATGAAAGCGCCGATGATGCAAACAGCAGACGGGCAAATTGAAGAGTCCTATTCCATT
TCCGCCGGGCTCGATTTCCCGTCCGTTGGGCCGCAACATGCGTACCTGAACAGCATCGGA
CGCGCGGATTATGTCTCCATTACCGATGATGAGGCGCTGGAAGCCTTCAAAACGTTGTGC
CGCCATGAGGGAATTATCCCGGCGCTGGAGTCCTCCCACGCGTTGGCGCACGCTCTGAAA
ATGATGCGCGAGCAGCCGGAAAAAGAGCAACTGCTGGTGGTCAATCTCTCTGGCCGCGGA
GATAAAGACATCTTTACCGTACACGATATCCTGAAAGCGCGAGGGGAAATCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A2K1
UniProtKB Entry NameTRPB_SALTY
GenBank Protein ID47942
GenBank Gene IDV01377
General References
  1. Crawford IP, Nichols BP, Yanofsky C: Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella typhimurium. J Mol Biol. 1980 Oct 5;142(4):489-502. [PubMed:7007651]
  2. 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]
  3. 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]
  4. 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]
  5. Selker E, Yanofsky C: Nucleotide sequence of the trpC-trpB intercistronic region from Salmonella typhimurium. J Mol Biol. 1979 May 15;130(2):135-43. [PubMed:381671]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]

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