ID   TRPA_VIBPA              Reviewed;         268 AA.
AC   P22095;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 135.
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=VP1961;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RX   PubMed=1773058; DOI=10.3109/10425179109020770;
RA   Crawford I.P., Han C.Y., Silverman M.;
RT   "Sequence and features of the tryptophan operon of Vibrio
RT   parahemolyticus.";
RL   DNA Seq. 1:189-196(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X17149; CAA35036.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC60224.1; -; Genomic_DNA.
DR   RefSeq; NP_798340.1; NC_004603.1.
DR   RefSeq; WP_005481690.1; NC_004603.1.
DR   AlphaFoldDB; P22095; -.
DR   SMR; P22095; -.
DR   STRING; 223926.28806953; -.
DR   EnsemblBacteria; BAC60224; BAC60224; BAC60224.
DR   GeneID; 1189472; -.
DR   KEGG; vpa:VP1961; -.
DR   PATRIC; fig|223926.6.peg.1876; -.
DR   eggNOG; COG0159; Bacteria.
DR   HOGENOM; CLU_016734_0_4_6; -.
DR   OMA; LVMTYWN; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002493; 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..268
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098871"
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"
FT   CONFLICT        204
FT                   /note="N -> D (in Ref. 1; CAA35036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="F -> L (in Ref. 1; CAA35036)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  28601 MW;  04B46ABE18558DD8 CRC64;
     MSRYEKMFAR LNEKNQGAFV PFVTVCDPNA EQSYKIMETL VESGADALEL GIPFSDPLAD
     GPTIQGANIR ALDSGATPDI CFEQIGKIRA KYPDLPIGLL MYANLVYSRG IESFYERCAK
     AGIDSVLIAD VPTNESAEFV AAAEKFGIHP IFIAPPTASD ETLKQVSELG GGYTYLLSRA
     GVTGAETKAN MPVDHMLEKL NQFNAPPALL GFGISEPAQV KQAIEAGAAG AISGSAVVKI
     IEAHVEQPQI MLDKLGEFVS AMKAATQK