ID   TRPA_CERS4              Reviewed;         263 AA.
AC   Q9X4E8; Q3IZM4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 116.
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}; OrderedLocusNames=RHOS4_24420;
GN   ORFNames=RSP_0831;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10511537; DOI=10.1093/genetics/153.2.525;
RA   Mackenzie C., Simmons A.E., Kaplan S.;
RT   "Multiple chromosomes in bacteria. The yin and yang of trp gene
RT   localization in Rhodobacter sphaeroides 2.4.1.";
RL   Genetics 153:525-538(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC       indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00131}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         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; EC=4.2.1.20;
CC         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. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; AF107094; AAD29264.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA80010.1; -; Genomic_DNA.
DR   RefSeq; WP_011338525.1; NZ_CP030271.1.
DR   RefSeq; YP_353911.1; NC_007493.2.
DR   AlphaFoldDB; Q9X4E8; -.
DR   SMR; Q9X4E8; -.
DR   STRING; 272943.RSP_0831; -.
DR   EnsemblBacteria; ABA80010; ABA80010; RSP_0831.
DR   GeneID; 57471160; -.
DR   KEGG; rsp:RSP_0831; -.
DR   PATRIC; fig|272943.9.peg.2793; -.
DR   eggNOG; COG0159; Bacteria.
DR   OMA; LVMTYWN; -.
DR   PhylomeDB; Q9X4E8; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002703; 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   PANTHER; PTHR43406; PTHR43406; 1.
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;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..263
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098835"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   263 AA;  27487 MW;  151DD8A4E140976D CRC64;
     MTRIDDTFRR LRAEGKKAFV AYIMAGDPDL ETSLAVMRGL PEAGVDIIEL GMPFTDPMAD
     GPTIQTAGQR ALEGGQTLTR TLEMVRAFRA ENAETPIVMM GYYNPIYARG VETFLAEATE
     AGIDGLIVVD LPPEEDAELC LPAQAAGLNF IRLATPTTDS RRLPKVLQNT SGFVYYVSIT
     GITGAAAAQA ADVAPEVARI KAATDLPVIV GFGITTPEAA QDLAGIADGC VVGSAIVKLV
     GEGRPVAEVL DRVAALAAGA HAA