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Protein

Tryptophan synthase beta chain

Gene

trpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.

Catalytic activityi

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

Cofactori

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional protein TrpGD (trpGD), Anthranilate synthase component 1 (trpE)
  2. Bifunctional protein TrpGD (trpGD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei62 – 621Nucleophile1 Publication
Active sitei86 – 861Proton donor1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • pyridoxal phosphate binding Source: EcoliWiki
  • tryptophan synthase activity Source: EcoCyc

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: EcoliWiki
  • tryptophan biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

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

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:TRYPSYN-BPROTEIN.
ECOL316407:JW1253-MONOMER.
MetaCyc:TRYPSYN-BPROTEIN.
BRENDAi4.2.1.20. 2026.
SABIO-RKP0A879.
UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase beta chain (EC:4.2.1.20)
Gene namesi
Name:trpB
Ordered Locus Names:b1261, JW1253
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11025. trpB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 397396Tryptophan synthase beta chainPRO_0000098948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

EPDiP0A879.
PaxDbiP0A879.
PRIDEiP0A879.

2D gel databases

SWISS-2DPAGEP0A879.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1123130,EBI-1123130

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259543. 9 interactions.
DIPiDIP-1036N.
IntActiP0A879. 8 interactions.
MINTiMINT-7711989.
STRINGi511145.b1261.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 213Combined sources
Helixi22 – 3716Combined sources
Helixi39 – 5113Combined sources
Beta strandi59 – 613Combined sources
Helixi63 – 664Combined sources
Beta strandi69 – 779Combined sources
Helixi78 – 803Combined sources
Helixi87 – 10014Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 12512Combined sources
Beta strandi129 – 1357Combined sources
Helixi136 – 1416Combined sources
Helixi143 – 1519Combined sources
Beta strandi155 – 1595Combined sources
Helixi166 – 18015Combined sources
Turni181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi189 – 1913Combined sources
Helixi197 – 2059Combined sources
Helixi207 – 22014Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi232 – 2343Combined sources
Helixi235 – 2417Combined sources
Helixi242 – 2443Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi250 – 25910Combined sources
Turni262 – 2643Combined sources
Helixi270 – 2734Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi282 – 2865Combined sources
Helixi311 – 3188Combined sources
Beta strandi321 – 3288Combined sources
Helixi329 – 34315Combined sources
Helixi349 – 36315Combined sources
Beta strandi370 – 3767Combined sources
Beta strandi378 – 3803Combined sources
Helixi381 – 3833Combined sources
Helixi384 – 39310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DH5X-ray2.90A1-397[»]
2DH6X-ray3.00A1-397[»]
ProteinModelPortaliP0A879.
SMRiP0A879. Positions 3-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A879.

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpB family.Curated

Phylogenomic databases

eggNOGiENOG4105CG0. Bacteria.
COG0133. LUCA.
HOGENOMiHOG000161710.
InParanoidiP0A879.
KOiK01696.
OMAiIPEMLYP.
OrthoDBiEOG6GFGH7.
PhylomeDBiP0A879.

Family and domain databases

HAMAPiMF_00133. Trp_synth_beta.
InterProiIPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PANTHERiPTHR10314:SF3. PTHR10314:SF3. 1 hit.
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00263. trpB. 1 hit.
PROSITEiPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLLNPYFG EFGGMYVPQI LMPALRQLEE AFVSAQKDPE FQAQFNDLLK
60 70 80 90 100
NYAGRPTALT KCQNITAGTN TTLYLKREDL LHGGAHKTNQ VLGQALLAKR
110 120 130 140 150
MGKTEIIAET GAGQHGVASA LASALLGLKC RIYMGAKDVE RQSPNVFRMR
160 170 180 190 200
LMGAEVIPVH SGSATLKDAC NEALRDWSGS YETAHYMLGT AAGPHPYPTI
210 220 230 240 250
VREFQRMIGE ETKAQILERE GRLPDAVIAC VGGGSNAIGM FADFINETNV
260 270 280 290 300
GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTE DGQIEESYSI
310 320 330 340 350
SAGLDFPSVG PQHAYLNSTG RADYVSITDD EALEAFKTLC LHEGIIPALE
360 370 380 390
SSHALAHALK MMRENPDKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI
Length:397
Mass (Da):42,983
Last modified:January 23, 2007 - v2
Checksum:i16CF49FBD738F06F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781E → K AA sequence (PubMed:6985892).Curated
Sequence conflicti365 – 3651N → Z AA sequence (PubMed:4552018).Curated
Sequence conflicti368 – 3692KE → BK AA sequence (PubMed:4552018).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti281 – 2811G → R in mutant TRPB8.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00365 Genomic DNA. Translation: CAA23663.1.
V00372 Genomic DNA. Translation: CAA23674.1.
U00096 Genomic DNA. Translation: AAC74343.1.
AP009048 Genomic DNA. Translation: BAA14793.1.
J01714 Genomic DNA. Translation: AAA57300.1.
U23489 Genomic DNA. Translation: AAB60034.1.
U23490 Genomic DNA. Translation: AAA65139.1.
U23492 Genomic DNA. Translation: AAA65151.1.
U23493 Genomic DNA. Translation: AAA65157.1.
U23500 Genomic DNA. Translation: AAA65175.1.
U25417 Genomic DNA. Translation: AAA73790.1.
U25418 Genomic DNA. Translation: AAA73796.1.
U25419 Genomic DNA. Translation: AAA73802.1.
U25422 Genomic DNA. Translation: AAA73820.1.
U25423 Genomic DNA. Translation: AAA73826.1.
U25426 Genomic DNA. Translation: AAA73838.1.
U25427 Genomic DNA. Translation: AAA73844.1.
U25428 Genomic DNA. Translation: AAA73850.1.
U25429 Genomic DNA. Translation: AAA73856.1.
PIRiH64873. TSECB.
RefSeqiNP_415777.1. NC_000913.3.
WP_000209520.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74343; AAC74343; b1261.
BAA14793; BAA14793; BAA14793.
GeneIDi945768.
KEGGiecj:JW1253.
eco:b1261.
PATRICi32117782. VBIEscCol129921_1311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00365 Genomic DNA. Translation: CAA23663.1.
V00372 Genomic DNA. Translation: CAA23674.1.
U00096 Genomic DNA. Translation: AAC74343.1.
AP009048 Genomic DNA. Translation: BAA14793.1.
J01714 Genomic DNA. Translation: AAA57300.1.
U23489 Genomic DNA. Translation: AAB60034.1.
U23490 Genomic DNA. Translation: AAA65139.1.
U23492 Genomic DNA. Translation: AAA65151.1.
U23493 Genomic DNA. Translation: AAA65157.1.
U23500 Genomic DNA. Translation: AAA65175.1.
U25417 Genomic DNA. Translation: AAA73790.1.
U25418 Genomic DNA. Translation: AAA73796.1.
U25419 Genomic DNA. Translation: AAA73802.1.
U25422 Genomic DNA. Translation: AAA73820.1.
U25423 Genomic DNA. Translation: AAA73826.1.
U25426 Genomic DNA. Translation: AAA73838.1.
U25427 Genomic DNA. Translation: AAA73844.1.
U25428 Genomic DNA. Translation: AAA73850.1.
U25429 Genomic DNA. Translation: AAA73856.1.
PIRiH64873. TSECB.
RefSeqiNP_415777.1. NC_000913.3.
WP_000209520.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DH5X-ray2.90A1-397[»]
2DH6X-ray3.00A1-397[»]
ProteinModelPortaliP0A879.
SMRiP0A879. Positions 3-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259543. 9 interactions.
DIPiDIP-1036N.
IntActiP0A879. 8 interactions.
MINTiMINT-7711989.
STRINGi511145.b1261.

2D gel databases

SWISS-2DPAGEP0A879.

Proteomic databases

EPDiP0A879.
PaxDbiP0A879.
PRIDEiP0A879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74343; AAC74343; b1261.
BAA14793; BAA14793; BAA14793.
GeneIDi945768.
KEGGiecj:JW1253.
eco:b1261.
PATRICi32117782. VBIEscCol129921_1311.

Organism-specific databases

EchoBASEiEB1018.
EcoGeneiEG11025. trpB.

Phylogenomic databases

eggNOGiENOG4105CG0. Bacteria.
COG0133. LUCA.
HOGENOMiHOG000161710.
InParanoidiP0A879.
KOiK01696.
OMAiIPEMLYP.
OrthoDBiEOG6GFGH7.
PhylomeDBiP0A879.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00044.
BioCyciEcoCyc:TRYPSYN-BPROTEIN.
ECOL316407:JW1253-MONOMER.
MetaCyc:TRYPSYN-BPROTEIN.
BRENDAi4.2.1.20. 2026.
SABIO-RKP0A879.

Miscellaneous databases

EvolutionaryTraceiP0A879.
PROiP0A879.

Family and domain databases

HAMAPiMF_00133. Trp_synth_beta.
InterProiIPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PANTHERiPTHR10314:SF3. PTHR10314:SF3. 1 hit.
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00263. trpB. 1 hit.
PROSITEiPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete nucleotide sequence of the tryptophan operon of Escherichia coli."
    Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M.
    Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons."
    Milkman R., Bridges M.M.
    Genetics 133:455-468(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella typhimurium."
    Crawford I.P., Nichols B.P., Yanofsky C.
    J. Mol. Biol. 142:489-502(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
  7. "Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli."
    Higgins W., Miles E.W., Fairwell T.
    J. Biol. Chem. 255:512-517(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-100, ACTIVE SITES.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  9. "Tryptophan synthetase beta 2 subunit. Primary structure of the pyridoxyl peptide from the Escherichia coli enzyme."
    Fluri R., Jackson L.E., Lee W.E., Crawford I.P.
    J. Biol. Chem. 246:6620-6624(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 77-99.
  10. "Tryptophan synthetase beta 2 subunit. Application of genetic analysis to the study of primary structure."
    Cotton R.G.H., Crawford I.P.
    J. Biol. Chem. 247:1883-1891(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 363-397.
  11. "Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive 'hinge' region diminishes substrate binding and alters solubility."
    Zhao G.-P., Somerville R.L.
    J. Biol. Chem. 267:526-541(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANT TRPB8.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiTRPB_ECOLI
AccessioniPrimary (citable) accession number: P0A879
Secondary accession number(s): P00932, P78146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.