ID   TRPA_AQUAE              Reviewed;         262 AA.
AC   O67502;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=aq_1548;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07458.1; -; Genomic_DNA.
DR   PIR; D70434; D70434.
DR   RefSeq; NP_214067.1; NC_000918.1.
DR   RefSeq; WP_010881005.1; NC_000918.1.
DR   PDB; 2EKC; X-ray; 2.00 A; A/B=1-262.
DR   PDBsum; 2EKC; -.
DR   AlphaFoldDB; O67502; -.
DR   SMR; O67502; -.
DR   STRING; 224324.aq_1548; -.
DR   EnsemblBacteria; AAC07458; AAC07458; aq_1548.
DR   KEGG; aae:aq_1548; -.
DR   PATRIC; fig|224324.8.peg.1201; -.
DR   eggNOG; COG0159; Bacteria.
DR   HOGENOM; CLU_016734_0_0_0; -.
DR   InParanoid; O67502; -.
DR   OMA; LVMTYWN; -.
DR   OrthoDB; 912786at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   EvolutionaryTrace; O67502; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Lyase; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..262
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098729"
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   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           30..42
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           62..73
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           78..91
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           103..109
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           111..120
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           133..145
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           160..169
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          174..179
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           192..204
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           218..225
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           235..242
FT                   /evidence="ECO:0007829|PDB:2EKC"
FT   HELIX           246..258
FT                   /evidence="ECO:0007829|PDB:2EKC"
SQ   SEQUENCE   262 AA;  29502 MW;  07BCC4AAF6F4B3AD CRC64;
     MGRISDKFTE LKEKREKALV SYLMVGYPDY ETSLKAFKEV LKNGTDILEI GFPFSDPVAD
     GPTIQVAHEV ALKNGIRFED VLELSETLRK EFPDIPFLLM TYYNPIFRIG LEKFCRLSRE
     KGIDGFIVPD LPPEEAEELK AVMKKYVLSF VPLGAPTSTR KRIKLICEAA DEMTYFVSVT
     GTTGAREKLP YERIKKKVEE YRELCDKPVV VGFGVSKKEH AREIGSFADG VVVGSALVKL
     AGQKKIEDLG NLVKELKEGL RE