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Tryptophan synthase alpha chain (EC 4.2.1.20)

 TRPA_ECOLI              Reviewed;         268 AA.
P0A877; P00928; Q47669;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 102.
RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131};
EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131};
Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131};
OrderedLocusNames=b1260, JW1252;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PROTEIN SEQUENCE.
PubMed=4863752;
Guest J.R., Drapeau G.R., Carlton B.C., Yanofsky C.;
"The amino acid sequence of the A protein (alpha subunit) of the
tryptophan synthetase of Escherichia coli.";
J. Biol. Chem. 242:5442-5446(1967).
[2]
PROTEIN SEQUENCE.
PubMed=388433; DOI=10.1073/pnas.76.10.5244;
Nichols B.P., Yanofsky C.;
"Nucleotide sequences of trpA of Salmonella typhimurium and
Escherichia coli: an evolutionary comparison.";
Proc. Natl. Acad. Sci. U.S.A. 76:5244-5248(1979).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7038627; DOI=10.1093/nar/9.24.6647;
Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E.,
Horowitz H., van Cleemput M., Wu A.M.;
"The complete nucleotide sequence of the tryptophan operon of
Escherichia coli.";
Nucleic Acids Res. 9:6647-6668(1981).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8095913;
Milkman R., Bridges M.M.;
"Molecular evolution of the Escherichia coli chromosome. IV. Sequence
comparisons.";
Genetics 133:455-468(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[8]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-225 (MUTANT TRPA46-ASP-PR3).
STRAIN=K12;
PubMed=2502189; DOI=10.1016/0300-9084(89)90089-8;
Tucker S.D., Murgola E.J., Pagel F.T.;
"Missense and nonsense suppressors can correct frameshift mutations.";
Biochimie 71:729-739(1989).
[10]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
-!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
of indoleglycerol phosphate to indole and glyceraldehyde 3-
phosphate.
-!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3-
phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
{ECO:0000255|HAMAP-Rule:MF_00131}.
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
Rule:MF_00131}.
-!- SUBUNIT: Tetramer of two alpha and two beta chains.
-!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
Rule:MF_00131}.
-----------------------------------------------------------------------
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EMBL; V00364; CAA23662.1; -; Genomic_DNA.
EMBL; V00372; CAA23675.1; -; Genomic_DNA.
EMBL; J01714; AAA57301.1; -; Genomic_DNA.
EMBL; U23489; AAB60035.1; -; Genomic_DNA.
EMBL; U23490; AAA65140.1; -; Genomic_DNA.
EMBL; U23491; AAA65146.1; -; Genomic_DNA.
EMBL; U23492; AAA65152.1; -; Genomic_DNA.
EMBL; U23494; AAA65164.1; -; Genomic_DNA.
EMBL; U25417; AAA73791.1; -; Genomic_DNA.
EMBL; U25418; AAA73797.1; -; Genomic_DNA.
EMBL; U25419; AAA73803.1; -; Genomic_DNA.
EMBL; U25420; AAA73809.1; -; Genomic_DNA.
EMBL; U25421; AAA73815.1; -; Genomic_DNA.
EMBL; U25422; AAA73821.1; -; Genomic_DNA.
EMBL; U00096; AAC74342.1; -; Genomic_DNA.
EMBL; AP009048; BAA14792.1; -; Genomic_DNA.
EMBL; X16698; CAA34671.1; -; Genomic_DNA.
PIR; E93746; TSECA.
RefSeq; NP_415776.1; NC_000913.3.
RefSeq; WP_000443067.1; NZ_LN832404.1.
PDB; 1V7Y; X-ray; 2.50 A; A/B=1-268.
PDB; 1WQ5; X-ray; 2.30 A; A/B=1-268.
PDB; 1XC4; X-ray; 2.80 A; A/B=1-268.
PDB; 1XCF; X-ray; 1.80 A; A/B=1-268.
PDBsum; 1V7Y; -.
PDBsum; 1WQ5; -.
PDBsum; 1XC4; -.
PDBsum; 1XCF; -.
DisProt; DP00252; -.
ProteinModelPortal; P0A877; -.
SMR; P0A877; -.
BioGrid; 4260129; 9.
DIP; DIP-35957N; -.
IntAct; P0A877; 6.
STRING; 316385.ECDH10B_1375; -.
SWISS-2DPAGE; P0A877; -.
PaxDb; P0A877; -.
PRIDE; P0A877; -.
EnsemblBacteria; AAC74342; AAC74342; b1260.
EnsemblBacteria; BAA14792; BAA14792; BAA14792.
GeneID; 946204; -.
KEGG; ecj:JW1252; -.
KEGG; eco:b1260; -.
PATRIC; fig|1411691.4.peg.1023; -.
EchoBASE; EB1017; -.
EcoGene; EG11024; trpA.
eggNOG; ENOG4105F6H; Bacteria.
eggNOG; COG0159; LUCA.
HOGENOM; HOG000223814; -.
InParanoid; P0A877; -.
KO; K01695; -.
PhylomeDB; P0A877; -.
BioCyc; EcoCyc:TRYPSYN-APROTEIN; -.
BioCyc; MetaCyc:TRYPSYN-APROTEIN; -.
BRENDA; 4.2.1.20; 2026.
SABIO-RK; P0A877; -.
UniPathway; UPA00035; UER00044.
EvolutionaryTrace; P0A877; -.
PRO; PR:P0A877; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016829; F:lyase activity; IDA:EcoCyc.
GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:EcoliWiki.
GO; GO:0000162; P:tryptophan biosynthetic process; IMP:EcoliWiki.
CDD; cd04724; Tryptophan_synthase_alpha; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00131; Trp_synth_alpha; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR011060; RibuloseP-bd_barrel.
InterPro; IPR018204; Trp_synthase_alpha_AS.
InterPro; IPR002028; Trp_synthase_suA.
Pfam; PF00290; Trp_syntA; 1.
SUPFAM; SSF51366; SSF51366; 1.
TIGRFAMs; TIGR00262; trpA; 1.
PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis;
Aromatic amino acid biosynthesis; Complete proteome;
Direct protein sequencing; Lyase; Reference proteome;
Tryptophan biosynthesis.
CHAIN 1 268 Tryptophan synthase alpha chain.
/FTId=PRO_0000098778.
ACT_SITE 49 49 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00131}.
ACT_SITE 60 60 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00131}.
VARIANT 209 224 LQGFGISAPDQVKAAI -> IAGFWYFRPGSGKSSD (in
mutant TrpA46-Asp-PR3).
HELIX 3 12 {ECO:0000244|PDB:1XCF}.
TURN 13 15 {ECO:0000244|PDB:1XCF}.
STRAND 18 24 {ECO:0000244|PDB:1XCF}.
STRAND 26 28 {ECO:0000244|PDB:1XCF}.
HELIX 30 43 {ECO:0000244|PDB:1XCF}.
STRAND 46 51 {ECO:0000244|PDB:1XCF}.
HELIX 70 73 {ECO:0000244|PDB:1WQ5}.
HELIX 78 91 {ECO:0000244|PDB:1XCF}.
STRAND 93 95 {ECO:0000244|PDB:1XCF}.
STRAND 97 101 {ECO:0000244|PDB:1XCF}.
HELIX 103 109 {ECO:0000244|PDB:1XCF}.
HELIX 111 121 {ECO:0000244|PDB:1XCF}.
STRAND 125 128 {ECO:0000244|PDB:1XCF}.
HELIX 133 135 {ECO:0000244|PDB:1XCF}.
HELIX 137 145 {ECO:0000244|PDB:1XCF}.
STRAND 149 151 {ECO:0000244|PDB:1V7Y}.
HELIX 160 169 {ECO:0000244|PDB:1XCF}.
STRAND 174 176 {ECO:0000244|PDB:1XCF}.
HELIX 179 181 {ECO:0000244|PDB:1WQ5}.
HELIX 193 202 {ECO:0000244|PDB:1XCF}.
STRAND 208 211 {ECO:0000244|PDB:1XCF}.
HELIX 217 225 {ECO:0000244|PDB:1XCF}.
STRAND 229 233 {ECO:0000244|PDB:1XCF}.
HELIX 236 242 {ECO:0000244|PDB:1XCF}.
TURN 244 246 {ECO:0000244|PDB:1WQ5}.
HELIX 248 264 {ECO:0000244|PDB:1XCF}.
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


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