ID   TRPC_PICTO              Reviewed;         250 AA.
AC   Q6L277;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00134};
DE            Short=IGPS {ECO:0000255|HAMAP-Rule:MF_00134};
DE            EC=4.1.1.48 {ECO:0000255|HAMAP-Rule:MF_00134};
GN   Name=trpC {ECO:0000255|HAMAP-Rule:MF_00134}; OrderedLocusNames=PTO0340;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00134};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00134}.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00134}.
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DR   EMBL; AE017261; AAT42925.1; -; Genomic_DNA.
DR   RefSeq; WP_011177141.1; NC_005877.1.
DR   AlphaFoldDB; Q6L277; -.
DR   SMR; Q6L277; -.
DR   STRING; 263820.PTO0340; -.
DR   EnsemblBacteria; AAT42925; AAT42925; PTO0340.
DR   GeneID; 2844852; -.
DR   KEGG; pto:PTO0340; -.
DR   PATRIC; fig|263820.9.peg.362; -.
DR   eggNOG; arCOG01088; Archaea.
DR   HOGENOM; CLU_034247_2_0_2; -.
DR   OMA; CEYRRER; -.
DR   OrthoDB; 98284at2157; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00331; IGPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00134_A; IGPS_A; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Lyase; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..250
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_0000154296"
SQ   SEQUENCE   250 AA;  28644 MW;  D10131D2C306FC7A CRC64;
     MIVDDIYKNN DKKILIKRNM RSRGILSMRS SIMNFNLNKK IGIIAEFKRR SPSGFVNNEN
     TDIFKYYDVI HNSIAGMSIL TEERYFNGNQ MDVVSVQRYN IPILIKDFVS NDEMIESSYM
     IGGDVILLIA DFLERDKIEM LNRKIKSLGM EALIEFHDLK AFERITTDEN VIIGYNRRNL
     KTLKIEDESF DAQDLIRSTG LLSVLESGIT SENILKMPRY NAMLIGSSIL SNDSVLKSAG
     MIKYDGFGYS