ID   TRPA_OPITP              Reviewed;         266 AA.
AC   B1ZT49;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Oter_2556;
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=452637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX   PubMed=21398538; DOI=10.1128/jb.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA   Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA   Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(2011).
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; CP001032; ACB75838.1; -; Genomic_DNA.
DR   RefSeq; WP_012375373.1; NC_010571.1.
DR   AlphaFoldDB; B1ZT49; -.
DR   SMR; B1ZT49; -.
DR   STRING; 452637.Oter_2556; -.
DR   EnsemblBacteria; ACB75838; ACB75838; Oter_2556.
DR   KEGG; ote:Oter_2556; -.
DR   eggNOG; COG0159; Bacteria.
DR   HOGENOM; CLU_016734_0_4_0; -.
DR   OMA; LVMTYWN; -.
DR   OrthoDB; 912786at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000007013; 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   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_1000095735"
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   266 AA;  28202 MW;  9D5280EF0832DEBA CRC64;
     MSRIAQAFQR AQAQNRAAFI AYLCAGDPNF DTSLAACRAV ITSGVDLLEL GVPFSDPLAD
     GLTNQLAAQR ALESGMTAAD VFRLVRRIRE FSEVPIVFYT YYNLVFAHGI DAYVRAAKEA
     GVDGLLTLDL PPEESDEVSA ACRAHGVQSV YIVAPTSPAE RIAKIAQAAT GFIYYVSREG
     VTGVQERVAA NIPEAVAAIR RHTALPVVVG FGISNREQVR QVAAVADGVV VGSALVNCIR
     ENLGSPERIT AKLAAVAGDL VAGTKR