TRPA_ECOLI
ID TRPA_ECOLI Reviewed; 268 AA.
AC P0A877; P00928; Q47669;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131};
GN OrderedLocusNames=b1260, JW1252;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4863752; DOI=10.1016/s0021-9258(18)99444-5;
RA Guest J.R., Drapeau G.R., Carlton B.C., Yanofsky C.;
RT "The amino acid sequence of the A protein (alpha subunit) of the tryptophan
RT synthetase of Escherichia coli.";
RL J. Biol. Chem. 242:5442-5446(1967).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=388433; DOI=10.1073/pnas.76.10.5244;
RA Nichols B.P., Yanofsky C.;
RT "Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia
RT coli: an evolutionary comparison.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:5244-5248(1979).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP PROTEIN SEQUENCE OF 1-12.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-225 (MUTANT TRPA46-ASP-PR3).
RC STRAIN=K12;
RX PubMed=2502189; DOI=10.1016/0300-9084(89)90089-8;
RA Tucker S.D., Murgola E.J., Pagel F.T.;
RT "Missense and nonsense suppressors can correct frameshift mutations.";
RL Biochimie 71:729-739(1989).
RN [10]
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 alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00131};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
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DR EMBL; V00364; CAA23662.1; -; Genomic_DNA.
DR EMBL; V00372; CAA23675.1; -; Genomic_DNA.
DR EMBL; J01714; AAA57301.1; -; Genomic_DNA.
DR EMBL; U23489; AAB60035.1; -; Genomic_DNA.
DR EMBL; U23490; AAA65140.1; -; Genomic_DNA.
DR EMBL; U23491; AAA65146.1; -; Genomic_DNA.
DR EMBL; U23492; AAA65152.1; -; Genomic_DNA.
DR EMBL; U23494; AAA65164.1; -; Genomic_DNA.
DR EMBL; U25417; AAA73791.1; -; Genomic_DNA.
DR EMBL; U25418; AAA73797.1; -; Genomic_DNA.
DR EMBL; U25419; AAA73803.1; -; Genomic_DNA.
DR EMBL; U25420; AAA73809.1; -; Genomic_DNA.
DR EMBL; U25421; AAA73815.1; -; Genomic_DNA.
DR EMBL; U25422; AAA73821.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74342.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14792.1; -; Genomic_DNA.
DR EMBL; X16698; CAA34671.1; -; Genomic_DNA.
DR PIR; E93746; TSECA.
DR RefSeq; NP_415776.1; NC_000913.3.
DR RefSeq; WP_000443067.1; NZ_SSZK01000031.1.
DR PDB; 1V7Y; X-ray; 2.50 A; A/B=1-268.
DR PDB; 1WQ5; X-ray; 2.30 A; A/B=1-268.
DR PDB; 1XC4; X-ray; 2.80 A; A/B=1-268.
DR PDB; 1XCF; X-ray; 1.80 A; A/B=1-268.
DR PDBsum; 1V7Y; -.
DR PDBsum; 1WQ5; -.
DR PDBsum; 1XC4; -.
DR PDBsum; 1XCF; -.
DR AlphaFoldDB; P0A877; -.
DR SMR; P0A877; -.
DR BioGRID; 4260129; 34.
DR ComplexPortal; CPX-3446; TrpAB tryptophan synthase complex.
DR DIP; DIP-35957N; -.
DR IntAct; P0A877; 6.
DR STRING; 511145.b1260; -.
DR BindingDB; P0A877; -.
DR ChEMBL; CHEMBL3885646; -.
DR SWISS-2DPAGE; P0A877; -.
DR jPOST; P0A877; -.
DR PaxDb; P0A877; -.
DR PRIDE; P0A877; -.
DR EnsemblBacteria; AAC74342; AAC74342; b1260.
DR EnsemblBacteria; BAA14792; BAA14792; BAA14792.
DR GeneID; 58388661; -.
DR GeneID; 946204; -.
DR KEGG; ecj:JW1252; -.
DR KEGG; eco:b1260; -.
DR PATRIC; fig|1411691.4.peg.1023; -.
DR EchoBASE; EB1017; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_4_6; -.
DR InParanoid; P0A877; -.
DR OMA; LVMTYWN; -.
DR PhylomeDB; P0A877; -.
DR BioCyc; EcoCyc:TRYPSYN-APROTEIN; -.
DR BioCyc; MetaCyc:TRYPSYN-APROTEIN; -.
DR BRENDA; 4.2.1.20; 2026.
DR SABIO-RK; P0A877; -.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; P0A877; -.
DR PRO; PR:P0A877; -.
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:0016829; F:lyase activity; IDA:EcoCyc.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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; cd04724; Tryptophan_synthase_alpha; 1.
DR DisProt; DP00252; -.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..268
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098778"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT VARIANT 209..224
FT /note="LQGFGISAPDQVKAAI -> IAGFWYFRPGSGKSSD (in mutant
FT TrpA46-Asp-PR3)"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1XCF"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1WQ5"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1V7Y"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1WQ5"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:1XCF"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1XCF"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:1XCF"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1WQ5"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:1XCF"
SQ SEQUENCE 268 AA; 28724 MW; 028223DB2B666CC6 CRC64;
MERYESLFAQ LKERKEGAFV PFVTLGDPGI EQSLKIIDTL IEAGADALEL GIPFSDPLAD
GPTIQNATLR AFAAGVTPAQ CFEMLALIRQ KHPTIPIGLL MYANLVFNKG IDEFYAQCEK
VGVDSVLVAD VPVEESAPFR QAALRHNVAP IFICPPNADD DLLRQIASYG RGYTYLLSRA
GVTGAENRAA LPLNHLVAKL KEYNAAPPLQ GFGISAPDQV KAAIDAGAAG AISGSAIVKI
IEQHINEPEK MLAALKVFVQ PMKAATRS
