ID   TRPC_STRT2              Reviewed;         255 AA.
AC   Q5M348;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=stu1590;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(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; CP000023; AAV61193.1; -; Genomic_DNA.
DR   RefSeq; WP_011226423.1; NC_006448.1.
DR   AlphaFoldDB; Q5M348; -.
DR   SMR; Q5M348; -.
DR   STRING; 264199.stu1590; -.
DR   EnsemblBacteria; AAV61193; AAV61193; stu1590.
DR   GeneID; 66899336; -.
DR   KEGG; stl:stu1590; -.
DR   PATRIC; fig|264199.4.peg.1562; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_1_9; -.
DR   OMA; RGPHDLI; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000001170; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..255
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_1000095901"
SQ   SEQUENCE   255 AA;  28188 MW;  FEBDB1A34FA0FA56 CRC64;
     MSKAFLPTIL EQKGKEVSQL VMEDLQPLRQ TYRLYDFLKS NQNKLQIISE VKKASPSMGD
     INLDVDIVAQ AKTYEENGAA MISVLTDEVF FKGDISYLKE ISTQVAIPTL AKDFIIDEKQ
     IVRSRNAGAT VILLIVAALP EARLKELYDF ATSLGLEVLV ETHNLPELEV AHRIGAEIIG
     VNNRNLVTFE TDINTSLELS THFKDKPVYI SESAIFTGQD AALVAPYFNG ILVGTALMTA
     DNVAKKVKEL QIDKG