ID   TRPC_STRP2              Reviewed;         255 AA.
AC   Q04IY7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=SPD_1599;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ55134.1; -; Genomic_DNA.
DR   RefSeq; WP_000076536.1; NC_008533.2.
DR   AlphaFoldDB; Q04IY7; -.
DR   SMR; Q04IY7; -.
DR   STRING; 373153.SPD_1599; -.
DR   EnsemblBacteria; ABJ55134; ABJ55134; SPD_1599.
DR   GeneID; 60233848; -.
DR   KEGG; spd:SPD_1599; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_1_9; -.
DR   OMA; RGPHDLI; -.
DR   OrthoDB; 1789381at2; -.
DR   BioCyc; SPNE373153:G1G6V-1729-MON; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000001452; 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_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..255
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_1000018555"
SQ   SEQUENCE   255 AA;  28915 MW;  D0025AE1CCB3C530 CRC64;
     MSQEFLARIL EQKAREVEQM KLEQIQPLRQ TYRLAEFLKN HQDCLQVIAE VKKASPSLGD
     INLDVDIVQQ AQTYEENGAV MISVLTDEVF FKGHLDYLRE ISSQVEIPTL NKDFIIDEKQ
     IIRARNAGAT VILLIVAALS EERLKELYDY ATELGLEVLV ETHNLAELEV AHRLGAEIIG
     VNNRNLTTFE VDLQTSVDLA PYFEEGRYYI SESAIFTGQD AERLAPYFNG ILVGTALMQA
     ENVVQRIKEL QIDKG