Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P0A2K1

- TRPB_SALTY

UniProt

P0A2K1 - TRPB_SALTY

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    2. tryptophan synthase activity Source: UniProtKB-HAMAP

    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.
    InterProiIPR001926. 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]
    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

    MTTLLNPYFG EFGGMYVPQI LMPALNQLEE AFVSAQKDPE FQAQFADLLK    50
    NYAGRPTALT KCQNITAGTR TTLYLKREDL LHGGAHKTNQ VLGQALLAKR 100
    MGKSEIIAET GAGQHGVASA LASALLGLKC RIYMGAKDVE RQSPNVFRMR 150
    LMGAEVIPVH SGSATLKDAC NEALRDWSGS YETAHYMLGT AAGPHPYPTI 200
    VREFQRMIGE ETKAQILDKE GRLPDAVIAC VGGGSNAIGM FADFINDTSV 250
    GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTA DGQIEESYSI 300
    SAGLDFPSVG PQHAYLNSIG RADYVSITDD EALEAFKTLC RHEGIIPALE 350
    SSHALAHALK MMREQPEKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI 397
    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 IPR001926. 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 ]
    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

    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 1, 2014
    This is version 80 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