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Tryptophan synthase alpha chain (EC 4.2.1.20)

 Q8KHV3_CHLTH            Unreviewed;       253 AA.
Q8KHV3;
01-OCT-2002, integrated into UniProtKB/TrEMBL.
01-OCT-2002, sequence version 1.
05-DEC-2018, entry version 107.
RecName: Full=Tryptophan synthase alpha chain {ECO:0000256|SAAS:SAAS01103933};
EC=4.2.1.20 {ECO:0000256|SAAS:SAAS01093371};
Name=trpA {ECO:0000313|EMBL:AAM19181.1};
Synonyms=trpA_1 {ECO:0000313|EMBL:CPR59386.1},
trpA_2 {ECO:0000313|EMBL:CPR59437.1};
ORFNames=ERS015770_00132 {ECO:0000313|EMBL:CPR59386.1},
ERS015770_00139 {ECO:0000313|EMBL:CPR59437.1},
ERS015772_00550 {ECO:0000313|EMBL:CPR52317.1},
ERS177788_00154 {ECO:0000313|EMBL:CQB85013.1};
Chlamydia trachomatis.
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=813 {ECO:0000313|EMBL:AAM19181.1};
[1] {ECO:0000313|EMBL:AAM19181.1}
NUCLEOTIDE SEQUENCE.
PubMed=12011099; DOI=10.1074/jbc.M203937200;
Fehlner-Gardiner C., Roshick C., Carlson J.H., Hughes S.,
Belland R.J., Caldwell H.D., McClarty G.;
"Molecular basis defining human Chlamydia trachomatis tissue tropism.
A possible role for tryptophan synthase.";
J. Biol. Chem. 277:26893-26903(2002).
[2] {ECO:0000313|EMBL:AFA51521.1}
NUCLEOTIDE SEQUENCE.
STRAIN=D2s {ECO:0000313|EMBL:AFA51521.1},
D83s {ECO:0000313|EMBL:AFA51522.1},
D84s {ECO:0000313|EMBL:AFA51523.1},
F38nl {ECO:0000313|EMBL:AFA51525.1},
Ja41nl {ECO:0000313|EMBL:AFA51527.1}, and
Ja47nl {ECO:0000313|EMBL:AFA51526.1};
PubMed=22123249; DOI=10.1128/JB.06268-11;
Srinivasan T., Bruno W.J., Wan R., Yen A., Duong J., Dean D.;
"In vitro recombinants of antibiotic-resistant Chlamydia trachomatis
strains have statistically more breakpoints than clinical recombinants
for the same sequenced loci and exhibit selection at unexpected
loci.";
J. Bacteriol. 194:617-626(2012).
[3] {ECO:0000313|EMBL:CPR52317.1, ECO:0000313|Proteomes:UP000038595, ECO:0000313|Proteomes:UP000044845}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SwabB1 {ECO:0000313|EMBL:CQB85013.1,
ECO:0000313|Proteomes:UP000038595},
SwabB4 {ECO:0000313|EMBL:CPR59386.1,
ECO:0000313|Proteomes:UP000044845}, and
SwabB8 {ECO:0000313|EMBL:CPR52317.1};
Murphy D.;
Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
of indoleglycerol phosphate to indole and glyceraldehyde 3-
phosphate. {ECO:0000256|SAAS:SAAS01111173}.
-!- CATALYTIC ACTIVITY:
Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
D-glyceraldehyde 3-phosphate + H2O + L-tryptophan;
Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776;
EC=4.2.1.20; Evidence={ECO:0000256|SAAS:SAAS01093367};
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 5/5.
{ECO:0000256|SAAS:SAAS01093362}.
-!- SUBUNIT: Tetramer of two alpha and two beta chains.
{ECO:0000256|SAAS:SAAS01111165}.
-!- SIMILARITY: Belongs to the TrpA family.
{ECO:0000256|RuleBase:RU003662, ECO:0000256|SAAS:SAAS01111172}.
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EMBL; AY096810; AAM19181.1; -; Genomic_DNA.
EMBL; AY096811; AAM19184.1; -; Genomic_DNA.
EMBL; AY096813; AAM19190.1; -; Genomic_DNA.
EMBL; JN795309; AFA51521.1; -; Genomic_DNA.
EMBL; JN795310; AFA51522.1; -; Genomic_DNA.
EMBL; JN795311; AFA51523.1; -; Genomic_DNA.
EMBL; JN795313; AFA51525.1; -; Genomic_DNA.
EMBL; JN795314; AFA51526.1; -; Genomic_DNA.
EMBL; JN795315; AFA51527.1; -; Genomic_DNA.
EMBL; CSTN01000006; CPR52317.1; -; Genomic_DNA.
EMBL; CSTQ01000003; CPR59386.1; -; Genomic_DNA.
EMBL; CSTQ01000003; CPR59437.1; -; Genomic_DNA.
EMBL; CTBL01000001; CQB85013.1; -; Genomic_DNA.
RefSeq; WP_009873062.1; NZ_CVNT01000001.1.
EnsemblBacteria; CPR52317; CPR52317; ERS015772_00550.
EnsemblBacteria; CPR59386; CPR59386; ERS015770_00132.
EnsemblBacteria; CPR59437; CPR59437; ERS015770_00139.
EnsemblBacteria; CQB85013; CQB85013; ERS177788_00154.
GeneID; 35554966; -.
PATRIC; fig|813.31.peg.191; -.
eggNOG; COG0159; LUCA.
UniPathway; UPA00035; UER00044.
Proteomes; UP000038595; Unassembled WGS sequence.
Proteomes; UP000044845; Unassembled WGS sequence.
GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
CDD; cd04724; Tryptophan_synthase_alpha; 1.
Gene3D; 3.20.20.70; -; 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.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS01093372};
Aromatic amino acid biosynthesis {ECO:0000256|SAAS:SAAS01093372};
Complete proteome {ECO:0000313|Proteomes:UP000038595,
ECO:0000313|Proteomes:UP000044845};
Lyase {ECO:0000256|SAAS:SAAS01093361, ECO:0000313|EMBL:CPR52317.1};
Tryptophan biosynthesis {ECO:0000256|SAAS:SAAS01093372}.
SEQUENCE 253 AA; 28100 MW; 5E0831111C8DF8F6 CRC64;
MSKLTQVFKQ TKPCIGYLTA GDGGTSYTIE AAKALIQGGV DILELGFPFS DPVADNPEIQ
VSHDRALAEN LTSETLLEIV EGIRAFNQEV PLILYSYYNP LLQRDLDYLR RLKDAGINGV
CVIDLPAPLS HGEKSPFFED LLAVGLDPIL LISAGTTPER MSLIQEYARG FLYYIPYQAT
RDSEVGIKEE FRKVREHFDL PIVDRRDICD KKEAAHVLNY SDGFIVKTAF VHQTTMDSSV
ETLTALAQTV IPG


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