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P0A2K1

- TRPB_SALTY

UniProt

P0A2K1 - TRPB_SALTY

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Protein

Tryptophan synthase beta chain

Gene

trpB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 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

Pyridoxal phosphate.

Pathwayi

GO - Molecular functioni

  1. tryptophan synthase activity Source: UniProtKB-HAMAP
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

BioCyciSENT99287:GCTI-1735-MONOMER.
UniPathwayiUPA00035; UER00044.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan synthase beta chain (EC:4.2.1.20)
Gene namesi
Name:trpB
Ordered Locus Names:STM1726
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 397396Tryptophan synthase beta chainPRO_0000098994Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiP0A2K1.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
trpAP0092922EBI-1028431,EBI-1028423

Protein-protein interaction databases

DIPiDIP-35707N.
IntActiP0A2K1. 1 interaction.
MINTiMINT-112874.
STRINGi99287.STM1726.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93
Beta strandi12 – 176
Helixi19 – 213
Helixi22 – 3615
Helixi39 – 5113
Turni52 – 543
Beta strandi59 – 613
Helixi63 – 664
Beta strandi69 – 779
Helixi78 – 803
Helixi87 – 10014
Beta strandi105 – 1139
Helixi114 – 12613
Beta strandi129 – 1357
Helixi136 – 1416
Helixi143 – 1519
Beta strandi155 – 1595
Beta strandi161 – 1633
Helixi166 – 18015
Turni181 – 1833
Beta strandi184 – 1863
Beta strandi189 – 1913
Helixi197 – 2059
Helixi207 – 22014
Beta strandi225 – 2306
Beta strandi232 – 2343
Helixi235 – 2417
Helixi242 – 2443
Beta strandi250 – 25910
Helixi262 – 2643
Helixi270 – 2734
Beta strandi274 – 2796
Beta strandi281 – 2866
Beta strandi290 – 2923
Helixi302 – 3043
Helixi311 – 3188
Beta strandi321 – 3288
Helixi329 – 34315
Helixi349 – 36416
Beta strandi370 – 3767
Beta strandi378 – 3803
Helixi381 – 3833
Helixi384 – 3929
Turni393 – 3953

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A2K1.
SMRiP0A2K1. Positions 2-395.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2K1.

Family & Domainsi

Sequence similaritiesi

Belongs to the TrpB family.Curated

Phylogenomic databases

HOGENOMiHOG000161710.
KOiK01696.
OMAiEFMTLLQ.
OrthoDBiEOG6GFGH7.
PhylomeDBiP0A2K1.

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.

P0A2K1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTLLNPYFG EFGGMYVPQI LMPALNQLEE AFVSAQKDPE FQAQFADLLK
60 70 80 90 100
NYAGRPTALT KCQNITAGTR TTLYLKREDL LHGGAHKTNQ VLGQALLAKR
110 120 130 140 150
MGKSEIIAET GAGQHGVASA LASALLGLKC RIYMGAKDVE RQSPNVFRMR
160 170 180 190 200
LMGAEVIPVH SGSATLKDAC NEALRDWSGS YETAHYMLGT AAGPHPYPTI
210 220 230 240 250
VREFQRMIGE ETKAQILDKE GRLPDAVIAC VGGGSNAIGM FADFINDTSV
260 270 280 290 300
GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTA DGQIEESYSI
310 320 330 340 350
SAGLDFPSVG PQHAYLNSIG RADYVSITDD EALEAFKTLC RHEGIIPALE
360 370 380 390
SSHALAHALK MMREQPEKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI
Length:397
Mass (Da):42,868
Last modified:January 23, 2007 - v2
Checksum:i73D210F5C6F2FEBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → R in CAA24667. (PubMed:7007651)Curated
Sequence conflicti34 – 341S → R in AAA27234. (PubMed:7007651)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA01156. TSEBBT.
RefSeqiNP_460685.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20644; AAL20644; STM1726.
GeneIDi1253245.
KEGGistm:STM1726.
PATRICi32381965. VBISalEnt20916_1822.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A01156. TSEBBT.
RefSeqi NP_460685.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A50 X-ray 2.30 B 2-397 [» ]
1A5A X-ray 1.90 B 1-395 [» ]
1A5B X-ray 2.00 B 1-395 [» ]
1A5S X-ray 2.30 B 1-397 [» ]
1BEU X-ray 1.90 B 1-395 [» ]
1BKS X-ray 2.20 B 1-397 [» ]
1C29 X-ray 2.30 B 1-397 [» ]
1C8V X-ray 2.20 B 1-397 [» ]
1C9D X-ray 2.30 B 1-397 [» ]
1CW2 X-ray 2.00 B 1-397 [» ]
1CX9 X-ray 2.30 B 1-397 [» ]
1FUY X-ray 2.25 B 2-397 [» ]
1K3U X-ray 1.70 B 2-397 [» ]
1K7E X-ray 2.30 B 2-397 [» ]
1K7F X-ray 1.90 B 2-397 [» ]
1K7X X-ray 1.70 B 2-397 [» ]
1K8X X-ray 1.90 B 1-397 [» ]
1K8Y X-ray 1.50 B 2-397 [» ]
1K8Z X-ray 1.70 B 2-397 [» ]
1KFB X-ray 1.90 B 2-397 [» ]
1KFC X-ray 1.50 B 1-397 [» ]
1KFE X-ray 1.75 B 2-395 [» ]
1KFJ X-ray 1.80 B 1-397 [» ]
1KFK X-ray 2.40 B 1-397 [» ]
1QOP X-ray 1.40 B 2-397 [» ]
1QOQ X-ray 1.80 B 2-397 [» ]
1TJP X-ray 1.50 B 2-397 [» ]
1TTP X-ray 2.30 B 1-397 [» ]
1TTQ X-ray 2.00 B 1-397 [» ]
1UBS X-ray 1.90 B 1-395 [» ]
1WBJ X-ray 1.50 B 2-397 [» ]
2CLE X-ray 1.50 B 2-397 [» ]
2CLF X-ray 1.70 B 2-397 [» ]
2CLH X-ray 1.70 B 2-397 [» ]
2CLI X-ray 1.70 B 2-397 [» ]
2CLK X-ray 1.50 B 2-397 [» ]
2CLL X-ray 1.60 B 2-397 [» ]
2CLM X-ray 1.51 B 2-397 [» ]
2CLO X-ray 1.50 B 2-397 [» ]
2J9X X-ray 1.90 B 2-397 [» ]
2J9Y X-ray 1.80 B 1-397 [» ]
2J9Z X-ray 1.80 B 1-397 [» ]
2RH9 X-ray 1.70 B 1-397 [» ]
2RHG X-ray 2.00 B 1-397 [» ]
2TRS X-ray 2.04 B 1-395 [» ]
2TSY X-ray 2.50 B 1-395 [» ]
2TYS X-ray 1.90 B 1-397 [» ]
2WSY X-ray 3.05 B 2-397 [» ]
3CEP X-ray 2.10 B 2-397 [» ]
3PR2 X-ray 1.85 B 3-393 [» ]
4HN4 X-ray 1.64 B 1-397 [» ]
4HPJ X-ray 1.45 B 1-397 [» ]
4HPX X-ray 1.65 B 1-397 [» ]
4HT3 X-ray 1.30 B 1-397 [» ]
4KKX X-ray 1.77 B 1-397 [» ]
ProteinModelPortali P0A2K1.
SMRi P0A2K1. Positions 2-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35707N.
IntActi P0A2K1. 1 interaction.
MINTi MINT-112874.
STRINGi 99287.STM1726.

Proteomic databases

PRIDEi P0A2K1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20644 ; AAL20644 ; STM1726 .
GeneIDi 1253245.
KEGGi stm:STM1726.
PATRICi 32381965. VBISalEnt20916_1822.

Phylogenomic databases

HOGENOMi HOG000161710.
KOi K01696.
OMAi EFMTLLQ.
OrthoDBi EOG6GFGH7.
PhylomeDBi P0A2K1.

Enzyme and pathway databases

UniPathwayi UPA00035 ; UER00044 .
BioCyci SENT99287:GCTI-1735-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A2K1.

Family and domain databases

HAMAPi MF_00133. Trp_synth_beta.
InterProi IPR006653. Trp_synth_b_CS.
IPR006654. Trp_synth_beta.
IPR023026. Trp_synth_beta/beta-like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view ]
PANTHERi PTHR10314:SF3. PTHR10314:SF3. 1 hit.
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
PIRSFi PIRSF001413. Trp_syn_beta. 1 hit.
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00263. trpB. 1 hit.
PROSITEi PS00168. TRP_SYNTHASE_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiTRPB_SALTY
AccessioniPrimary (citable) accession number: P0A2K1
Secondary accession number(s): P00933, Q56141
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 81 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3