(data stored in ACNUC7421 zone)

SWISSPROT: TRPA_PARDP

ID   TRPA_PARDP              Reviewed;         265 AA.
AC   A1AYV3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=Pden_0333;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL68447.1; -; Genomic_DNA.
DR   RefSeq; WP_011746680.1; NC_008686.1.
DR   SMR; A1AYV3; -.
DR   STRING; 318586.Pden_0333; -.
DR   PRIDE; A1AYV3; -.
DR   EnsemblBacteria; ABL68447; ABL68447; Pden_0333.
DR   KEGG; pde:Pden_0333; -.
DR   eggNOG; ENOG4105F6H; Bacteria.
DR   eggNOG; COG0159; LUCA.
DR   HOGENOM; HOG000223815; -.
DR   KO; K01695; -.
DR   OMA; DYPPEEC; -.
DR   BioCyc; PDEN318586:G1GW1-327-MONOMER; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AYV3.
DR   SWISS-2DPAGE; A1AYV3.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN         1    265       Tryptophan synthase alpha chain.
FT                                /FTId=PRO_1000018244.
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   265 AA;  27511 MW;  0205285EE6714A48 CRC64;
     MSRIDDTFAR LSETGGKAFV AYMMGCDPDF DTSLQIMRGL PGAGVDIIEL GMPFTDPMAD
     GATIQAAGQR ALAAGGSVSR VLDMVRAFRR DDDATPIVLM GYYNPIYARQ GGVDRFITEA
     VEAGVDGLIV VDLPPEEDAE LCLPAREAGL NFIRLATPTT DDRRLPAVVR NTSGFVYYVS
     VTGITGGPAA NAAEVAPEVA RIRAAAKLPV VVGFGISTPE AAQAVAGVAD GCVVGSAIVK
     LIGEGRPVPE ILSFVADLAQ GAHSA
//

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