TRPB_ECOLI
ID TRPB_ECOLI Reviewed; 397 AA.
AC P0A879; P00932; P78146;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=b1261, JW1253;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7038627; DOI=10.1093/nar/9.24.6647;
RA Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E.,
RA Horowitz H., van Cleemput M., Wu A.M.;
RT "The complete nucleotide sequence of the tryptophan operon of Escherichia
RT coli.";
RL Nucleic Acids Res. 9:6647-6668(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8095913; DOI=10.1093/genetics/133.3.455;
RA Milkman R., Bridges M.M.;
RT "Molecular evolution of the Escherichia coli chromosome. IV. Sequence
RT comparisons.";
RL Genetics 133:455-468(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
RX PubMed=7007651; DOI=10.1016/0022-2836(80)90259-4;
RA Crawford I.P., Nichols B.P., Yanofsky C.;
RT "Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella
RT typhimurium.";
RL J. Mol. Biol. 142:489-502(1980).
RN [7]
RP PROTEIN SEQUENCE OF 2-100, AND ACTIVE SITES.
RX PubMed=6985892; DOI=10.1016/s0021-9258(19)86203-8;
RA Higgins W., Miles E.W., Fairwell T.;
RT "Location of three active site residues in the NH2-terminal sequence of the
RT beta 2 subunit tryptophan synthase from Escherichia coli.";
RL J. Biol. Chem. 255:512-517(1980).
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 77-99.
RX PubMed=4943677; DOI=10.1016/s0021-9258(19)34159-6;
RA Fluri R., Jackson L.E., Lee W.E., Crawford I.P.;
RT "Tryptophan synthetase beta 2 subunit. Primary structure of the pyridoxyl
RT peptide from the Escherichia coli enzyme.";
RL J. Biol. Chem. 246:6620-6624(1971).
RN [10]
RP PROTEIN SEQUENCE OF 363-397.
RX PubMed=4552018; DOI=10.1016/s0021-9258(19)45553-1;
RA Cotton R.G.H., Crawford I.P.;
RT "Tryptophan synthetase beta 2 subunit. Application of genetic analysis to
RT the study of primary structure.";
RL J. Biol. Chem. 247:1883-1891(1972).
RN [11]
RP MUTANT TRPB8.
RX PubMed=1309752; DOI=10.1016/s0021-9258(18)48527-4;
RA Zhao G.-P., Somerville R.L.;
RT "Genetic and biochemical characterization of the trpB8 mutation of
RT Escherichia coli tryptophan synthase. An amino acid switch at the sharp
RT turn of the trypsin-sensitive 'hinge' region diminishes substrate binding
RT and alters solubility.";
RL J. Biol. Chem. 267:526-541(1992).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- INTERACTION:
CC P0A879; P0A879: trpB; NbExp=2; IntAct=EBI-1123130, EBI-1123130;
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V00365; CAA23663.1; -; Genomic_DNA.
DR EMBL; V00372; CAA23674.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74343.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14793.1; -; Genomic_DNA.
DR EMBL; J01714; AAA57300.1; -; Genomic_DNA.
DR EMBL; U23489; AAB60034.1; -; Genomic_DNA.
DR EMBL; U23490; AAA65139.1; -; Genomic_DNA.
DR EMBL; U23492; AAA65151.1; -; Genomic_DNA.
DR EMBL; U23493; AAA65157.1; -; Genomic_DNA.
DR EMBL; U23500; AAA65175.1; -; Genomic_DNA.
DR EMBL; U25417; AAA73790.1; -; Genomic_DNA.
DR EMBL; U25418; AAA73796.1; -; Genomic_DNA.
DR EMBL; U25419; AAA73802.1; -; Genomic_DNA.
DR EMBL; U25422; AAA73820.1; -; Genomic_DNA.
DR EMBL; U25423; AAA73826.1; -; Genomic_DNA.
DR EMBL; U25426; AAA73838.1; -; Genomic_DNA.
DR EMBL; U25427; AAA73844.1; -; Genomic_DNA.
DR EMBL; U25428; AAA73850.1; -; Genomic_DNA.
DR EMBL; U25429; AAA73856.1; -; Genomic_DNA.
DR PIR; H64873; TSECB.
DR RefSeq; NP_415777.1; NC_000913.3.
DR RefSeq; WP_000209520.1; NZ_STEB01000005.1.
DR PDB; 2DH5; X-ray; 2.90 A; A=1-397.
DR PDB; 2DH6; X-ray; 3.00 A; A=1-397.
DR PDBsum; 2DH5; -.
DR PDBsum; 2DH6; -.
DR AlphaFoldDB; P0A879; -.
DR SMR; P0A879; -.
DR BioGRID; 4259543; 47.
DR BioGRID; 850135; 1.
DR ComplexPortal; CPX-3446; TrpAB tryptophan synthase complex.
DR DIP; DIP-1036N; -.
DR IntAct; P0A879; 8.
DR MINT; P0A879; -.
DR STRING; 511145.b1261; -.
DR BindingDB; P0A879; -.
DR ChEMBL; CHEMBL3885646; -.
DR SWISS-2DPAGE; P0A879; -.
DR jPOST; P0A879; -.
DR PaxDb; P0A879; -.
DR PRIDE; P0A879; -.
DR ABCD; P0A879; 1 sequenced antibody.
DR EnsemblBacteria; AAC74343; AAC74343; b1261.
DR EnsemblBacteria; BAA14793; BAA14793; BAA14793.
DR GeneID; 58388660; -.
DR GeneID; 945768; -.
DR KEGG; ecj:JW1253; -.
DR KEGG; eco:b1261; -.
DR PATRIC; fig|1411691.4.peg.1022; -.
DR EchoBASE; EB1018; -.
DR eggNOG; COG0133; Bacteria.
DR InParanoid; P0A879; -.
DR OMA; HGMKSYF; -.
DR PhylomeDB; P0A879; -.
DR BioCyc; EcoCyc:TRYPSYN-BPROTEIN; -.
DR BioCyc; MetaCyc:TRYPSYN-BPROTEIN; -.
DR BRENDA; 4.2.1.20; 2026.
DR SABIO-RK; P0A879; -.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; P0A879; -.
DR PRO; PR:P0A879; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki.
DR GO; GO:0004834; F:tryptophan synthase activity; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:ComplexPortal.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00263; trpB; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6985892,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..397
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098948"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:6985892"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:6985892"
FT MOD_RES 87
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VARIANT 281
FT /note="G -> R (in mutant TRPB8)"
FT CONFLICT 78
FT /note="E -> K (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="N -> Z (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="KE -> BK (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:2DH5"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:2DH5"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:2DH5"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:2DH5"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:2DH5"
SQ SEQUENCE 397 AA; 42983 MW; 16CF49FBD738F06F CRC64;
MTTLLNPYFG EFGGMYVPQI LMPALRQLEE AFVSAQKDPE FQAQFNDLLK NYAGRPTALT
KCQNITAGTN TTLYLKREDL LHGGAHKTNQ VLGQALLAKR MGKTEIIAET GAGQHGVASA
LASALLGLKC RIYMGAKDVE RQSPNVFRMR LMGAEVIPVH SGSATLKDAC NEALRDWSGS
YETAHYMLGT AAGPHPYPTI VREFQRMIGE ETKAQILERE GRLPDAVIAC VGGGSNAIGM
FADFINETNV GLIGVEPGGH GIETGEHGAP LKHGRVGIYF GMKAPMMQTE DGQIEESYSI
SAGLDFPSVG PQHAYLNSTG RADYVSITDD EALEAFKTLC LHEGIIPALE SSHALAHALK
MMRENPDKEQ LLVVNLSGRG DKDIFTVHDI LKARGEI
