(data stored in ACNUC7421 zone)

SWISSPROT: TRPA_PSEAB

ID   TRPA_PSEAB              Reviewed;         268 AA.
AC   Q02V45;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 63.
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=PA14_00440;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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: L-serine + 1-C-(indol-3-yl)glycerol 3-
CC       phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
CC       {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; CP000438; ABJ14992.1; -; Genomic_DNA.
DR   RefSeq; WP_003097337.1; NC_008463.1.
DR   ProteinModelPortal; Q02V45; -.
DR   SMR; Q02V45; -.
DR   EnsemblBacteria; ABJ14992; ABJ14992; PA14_00440.
DR   KEGG; pau:PA14_00440; -.
DR   HOGENOM; HOG000223815; -.
DR   KO; K01695; -.
DR   OMA; DYPPEEC; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
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; Q02V45.
DR   SWISS-2DPAGE; Q02V45.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Tryptophan biosynthesis.
FT   CHAIN         1    268       Tryptophan synthase alpha chain.
FT                                /FTId=PRO_1000018253.
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   268 AA;  28488 MW;  6CC7002524A9BBAD CRC64;
     MSRLQTRFAQ LKQENRAALV TFVTAGDPDY ASSLEILKGL PAAGADVIEL GMPFTDPMAD
     GPAIQLANIR ALDGGQTLAR TLQMVREFRS GDSETPLVLM GYFNPIHHYG VERFIAEAKE
     VGVDGLIVVD LPPEHNEDLC HPAQAAGLDF IRLTTPTTGD QRLPTVLEGS SGFVYYVSVA
     GVTGANAATL EHVEEAVARL RRHTDLPIGI GFGIRSAEHA AAVARLADGV VVGSALIDRI
     AKARDNAQAV KDVLALCGEL AEGVRNAR
//

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