ID   TRPC_PSEA8              Reviewed;         278 AA.
AC   B7V609;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=PLES_06301;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
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; FM209186; CAW25357.1; -; Genomic_DNA.
DR   RefSeq; WP_003085205.1; NC_011770.1.
DR   AlphaFoldDB; B7V609; -.
DR   SMR; B7V609; -.
DR   PRIDE; B7V609; -.
DR   KEGG; pag:PLES_06301; -.
DR   HOGENOM; CLU_034247_2_0_6; -.
DR   OMA; RGPHDLI; -.
DR   UniPathway; UPA00035; UER00043.
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_B; IGPS_B; 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; Tryptophan biosynthesis.
FT   CHAIN           1..278
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_1000198782"
SQ   SEQUENCE   278 AA;  30333 MW;  4011EF45378B55F8 CRC64;
     MSVPTVLQKI LARKAEEVAE RRARVNLAEV ERLARSADAP RGFANALLER AKRKEPAVIA
     EIKKASPSKG VLREHFVPAE IARSYEAGGA ACLSVLTDVD FFQGADAYLK EARAACALPV
     IRKDFMIDPY QIVEARAIGA DCILLIVSAL DDVLMAELAA TAKSVGLDVL VEVHDGTELE
     RALKTLDTPL VGINNRNLHT FEVSLETTLD LLPEIPRDRL VVTESGILNR ADVELMEVSE
     VYAFLVGEAF MRADDPGLEL KRLFFQERGG VVLGADPD