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
- Functionstryptophan 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
- PALP (PF00291)
- 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
Resource Link UniProtKB ID P0A2K1 UniProtKB Entry Name TRPB_SALTY GenBank Protein ID 47942 GenBank Gene ID V01377 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB07732 2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL DIHYDROGEN PHOSPHATE experimental unknown Details DB07745 2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE experimental unknown Details DB07748 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE experimental unknown Details DB07773 5-FLUOROINDOLE PROPANOL PHOSPHATE experimental unknown Details DB07890 4-(2-HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID experimental unknown Details DB07894 4-(2-HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID experimental unknown Details DB07925 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID experimental unknown Details DB07951 N-(indole-3-acetyl)-L-aspartic acid experimental unknown Details DB07952 N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID experimental unknown Details DB07953 N-[1H-INDOL-3-YL-ACETYL]VALINE ACID experimental unknown Details DB04143 Indole-3-Glycerol Phosphate experimental unknown Details DB03171 Indole-3-Propanol Phosphate experimental unknown Details