(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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