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P0A2K1 (TRPB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan synthase beta chain

EC=4.2.1.20
Gene names
Name:trpB
Ordered Locus Names:STM1726
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. HAMAP-Rule MF_00133

Catalytic activity

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O. HAMAP-Rule MF_00133

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule MF_00133

Subunit structure

Tetramer of two alpha and two beta chains.

Sequence similarities

Belongs to the TrpB family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

trpAP0092922EBI-1028431,EBI-1028423

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00133
Chain2 – 397396Tryptophan synthase beta chain HAMAP-Rule MF_00133
PRO_0000098994

Amino acid modifications

Modified residue871N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00133

Experimental info

Sequence conflict341S → R in CAA24667. Ref.1
Sequence conflict341S → R in AAA27234. Ref.1

Secondary structure

........................................................................... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A2K1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 73D210F5C6F2FEBD

FASTA39742,868
        10         20         30         40         50         60 
MTTLLNPYFG EFGGMYVPQI LMPALNQLEE AFVSAQKDPE FQAQFADLLK NYAGRPTALT 

        70         80         90        100        110        120 
KCQNITAGTR TTLYLKREDL LHGGAHKTNQ VLGQALLAKR MGKSEIIAET GAGQHGVASA 

       130        140        150        160        170        180 
LASALLGLKC RIYMGAKDVE RQSPNVFRMR LMGAEVIPVH SGSATLKDAC NEALRDWSGS 

       190        200        210        220        230        240 
YETAHYMLGT AAGPHPYPTI VREFQRMIGE ETKAQILDKE GRLPDAVIAC VGGGSNAIGM 

       250        260        270        280        290        300 
FADFINDTSV GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTA DGQIEESYSI 

       310        320        330        340        350        360 
SAGLDFPSVG PQHAYLNSIG RADYVSITDD EALEAFKTLC RHEGIIPALE SSHALAHALK 

       370        380        390 
MMREQPEKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., 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. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"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] OF 375-397.
[4]"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] OF 375-397.
[5]"Nucleotide sequence of the trpC-trpB intercistronic region from Salmonella typhimurium."
Selker E., Yanofsky C.
J. Mol. Biol. 130:135-143(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[6]"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).
[7]"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) OF WILD TYPE AND TYR-87 MUTANTS IN COMPLEX WITH L-SERINE, PYRIDOXAL PHOSPHATE AT LYS-87.
[8]"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).
[9]"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).
[10]"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).
[11]"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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01377 Genomic DNA. Translation: CAA24667.1.
J01810 Genomic DNA. Translation: AAA27234.1.
AE006468 Genomic DNA. Translation: AAL20644.1.
V01376 Genomic DNA. Translation: CAA24665.1.
V00364 Genomic DNA. Translation: CAA23661.1.
M24299 Genomic DNA. Translation: AAA99293.1.
PIRTSEBBT. A01156.
RefSeqNP_460685.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A50X-ray2.30B2-397[»]
1A5AX-ray1.90B1-395[»]
1A5BX-ray2.00B1-395[»]
1A5SX-ray2.30B1-397[»]
1BEUX-ray1.90B1-395[»]
1BKSX-ray2.20B1-397[»]
1C29X-ray2.30B1-397[»]
1C8VX-ray2.20B1-397[»]
1C9DX-ray2.30B1-397[»]
1CW2X-ray2.00B1-397[»]
1CX9X-ray2.30B1-397[»]
1FUYX-ray2.25B2-397[»]
1K3UX-ray1.70B2-397[»]
1K7EX-ray2.30B2-397[»]
1K7FX-ray1.90B2-397[»]
1K7XX-ray1.70B2-397[»]
1K8XX-ray1.90B1-397[»]
1K8YX-ray1.50B2-397[»]
1K8ZX-ray1.70B2-397[»]
1KFBX-ray1.90B2-397[»]
1KFCX-ray1.50B1-397[»]
1KFEX-ray1.75B2-395[»]
1KFJX-ray1.80B1-397[»]
1KFKX-ray2.40B1-397[»]
1QOPX-ray1.40B2-397[»]
1QOQX-ray1.80B2-397[»]
1TJPX-ray1.50B2-397[»]
1TTPX-ray2.30B1-397[»]
1TTQX-ray2.00B1-397[»]
1UBSX-ray1.90B1-395[»]
1WBJX-ray1.50B2-397[»]
2CLEX-ray1.50B2-397[»]
2CLFX-ray1.70B2-397[»]
2CLHX-ray1.70B2-397[»]
2CLIX-ray1.70B2-397[»]
2CLKX-ray1.50B2-397[»]
2CLLX-ray1.60B2-397[»]
2CLMX-ray1.51B2-397[»]
2CLOX-ray1.50B2-397[»]
2J9XX-ray1.90B2-397[»]
2J9YX-ray1.80B1-397[»]
2J9ZX-ray1.80B1-397[»]
2RH9X-ray1.70B1-397[»]
2RHGX-ray2.00B1-397[»]
2TRSX-ray2.04B1-395[»]
2TSYX-ray2.50B1-395[»]
2TYSX-ray1.90B1-397[»]
2WSYX-ray3.05B2-397[»]
3CEPX-ray2.10B2-397[»]
3PR2X-ray1.85B3-393[»]
4HN4X-ray1.64B1-397[»]
4HPJX-ray1.45B1-397[»]
4HPXX-ray1.65B1-397[»]
4HT3X-ray1.30B1-397[»]
4KKXX-ray1.77B1-397[»]
ProteinModelPortalP0A2K1.
SMRP0A2K1. Positions 2-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35707N.
IntActP0A2K1. 1 interaction.
MINTMINT-112874.
STRING99287.STM1726.

Proteomic databases

PRIDEP0A2K1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20644; AAL20644; STM1726.
GeneID1253245.
KEGGstm:STM1726.
PATRIC32381965. VBISalEnt20916_1822.

Phylogenomic databases

HOGENOMHOG000161710.
KOK01696.
OMAEFMTLLQ.
OrthoDBEOG6GFGH7.
PhylomeDBP0A2K1.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1735-MONOMER.
UniPathwayUPA00035; UER00044.

Family and domain databases

HAMAPMF_00133. Trp_synth_beta.
InterProIPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
IPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
[Graphical view]
PANTHERPTHR10314:SF3. PTHR10314:SF3. 1 hit.
PfamPF00291. PALP. 1 hit.
[Graphical view]
PIRSFPIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR00263. trpB. 1 hit.
PROSITEPS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A2K1.

Entry information

Entry nameTRPB_SALTY
AccessionPrimary (citable) accession number: P0A2K1
Secondary accession number(s): P00933, Q56141
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways