(data stored in ACNUC7421 zone)
SWISSPROT: TRPA_PSEU2
ID TRPA_PSEU2 Reviewed; 269 AA.
AC Q500R5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 08-MAY-2019, entry version 80.
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=Psyr_0033;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae
RT pv. syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage
CC of indoleglycerol phosphate to indole and glyceraldehyde 3-
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine =
CC D-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;
CC EC=4.2.1.20; 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 {ECO:0000255|HAMAP-Rule:MF_00131}.
CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00131}.
DR EMBL; CP000075; AAY35107.1; -; Genomic_DNA.
DR RefSeq; WP_003318459.1; NC_007005.1.
DR RefSeq; YP_233145.1; NC_007005.1.
DR SMR; Q500R5; -.
DR STRING; 205918.Psyr_0033; -.
DR EnsemblBacteria; AAY35107; AAY35107; Psyr_0033.
DR GeneID; 3365508; -.
DR KEGG; psb:Psyr_0033; -.
DR PATRIC; fig|205918.7.peg.32; -.
DR eggNOG; ENOG4105F6H; Bacteria.
DR eggNOG; COG0159; LUCA.
DR HOGENOM; HOG000223815; -.
DR KO; K01695; -.
DR OMA; DYPPEEC; -.
DR BioCyc; PSYR205918:G1G4J-33-MONOMER; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
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 Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
DR PRODOM; Q500R5.
DR SWISS-2DPAGE; Q500R5.
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Lyase; Tryptophan biosynthesis.
FT CHAIN 1 269 Tryptophan synthase alpha chain.
FT /FTId=PRO_1000018259.
FT ACT_SITE 49 49 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_00131}.
FT ACT_SITE 60 60 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_00131}.
SQ SEQUENCE 269 AA; 28449 MW; 84C3FE9DF8487B03 CRC64;
MSRLEHRFAQ LKTEGRAALV TFITAGDPGY DTSLKVLKGL PAAGADVIEL GMPFTDPMAD
GVAIQLATLR ALDAGQTLQK TLQMVSEFRV DDQTTPIVLM GYYNPIHRFG VEAFVAQAKE
AGVDGLIIVD LPPEHDAELA TPAQASGIDF IRLTTPTTDD ARLPRVLERS SGFVYYVSVA
GVTGAGSATT EHVTEAIARL RRHTDLPISV GFGIRTPEQA AAIARLADGV VVGSAFVDKI
ASAESPEHAI DGVLTLCAAL AEGVRSARR
//
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