ID   TRPA_LEPBP              Reviewed;         266 AA.
AC   Q5MI53; B0SM56;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=LEPBI_I2607;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15838052; DOI=10.1128/jb.187.9.3249-3254.2005;
RA   Louvel H., Saint Girons I., Picardeau M.;
RT   "Isolation and characterization of FecA- and FeoB-mediated iron acquisition
RT   systems of the spirochete Leptospira biflexa by random insertional
RT   mutagenesis.";
RL   J. Bacteriol. 187:3249-3254(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; AY828567; AAV85863.1; -; Genomic_DNA.
DR   EMBL; CP000786; ABZ98686.1; -; Genomic_DNA.
DR   RefSeq; WP_012389546.1; NC_010602.1.
DR   AlphaFoldDB; Q5MI53; -.
DR   SMR; Q5MI53; -.
DR   STRING; 456481.LEPBI_I2607; -.
DR   KEGG; lbi:LEPBI_I2607; -.
DR   HOGENOM; CLU_016734_0_0_12; -.
DR   OMA; LVMTYWN; -.
DR   OrthoDB; 912786at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS12825-MON; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001847; Chromosome I.
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..266
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098800"
FT   ACT_SITE        47
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ   SEQUENCE   266 AA;  29698 MW;  3CC5D553249061F4 CRC64;
     MSKIKELFES GKFKSAFIPY FTLGDPNYND SIEFGKTILD GGADILELGI PFSDPVADGP
     VIQRAVARSL KNKFSFDEIF RVTKQIHLHK QETPLVYLTY FNPIYHCGIT KFLDNAKDSG
     VVGLVIPDLP FDTIESETLF QELRLRDMDL IHLVTPASTK KRIEALRKTS TGFIYYVTSF
     GVTGERREFS VDLKERIRFL KDTIQLPICA GFGISTPEQA SQIAGYADGI IIGSAIQRVI
     EENGQDASKA KNVLADYITK IRASIS