Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A2K1

- TRPB_SALTY

UniProt

P0A2K1 - TRPB_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 – 93Combined sources
Beta strandi12 – 176Combined sources
Helixi19 – 213Combined sources
Helixi22 – 3615Combined sources
Helixi39 – 5113Combined sources
Turni52 – 543Combined sources
Beta strandi59 – 613Combined sources
Helixi63 – 664Combined sources
Beta strandi69 – 779Combined sources
Helixi78 – 803Combined sources
Helixi87 – 10014Combined sources
Beta strandi105 – 1139Combined sources
Helixi114 – 12613Combined sources
Beta strandi129 – 1357Combined sources
Helixi136 – 1416Combined sources
Helixi143 – 1519Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi161 – 1633Combined 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 strandi250 – 25910Combined sources
Helixi262 – 2643Combined sources
Helixi270 – 2734Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi290 – 2923Combined sources
Helixi302 – 3043Combined sources
Helixi311 – 3188Combined sources
Beta strandi321 – 3288Combined sources
Helixi329 – 34315Combined sources
Helixi349 – 36416Combined sources
Beta strandi370 – 3767Combined sources
Beta strandi378 – 3803Combined sources
Helixi381 – 3833Combined sources
Helixi384 – 3929Combined sources
Turni393 – 3953Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 82 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