ID   TRPC_STAES              Reviewed;         262 AA.
AC   Q8CPB2;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=SE_1051;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04648.1; -; Genomic_DNA.
DR   RefSeq; NP_764606.1; NC_004461.1.
DR   RefSeq; WP_002485159.1; NZ_WBME01000002.1.
DR   AlphaFoldDB; Q8CPB2; -.
DR   SMR; Q8CPB2; -.
DR   STRING; 176280.SE_1051; -.
DR   EnsemblBacteria; AAO04648; AAO04648; SE_1051.
DR   KEGG; sep:SE_1051; -.
DR   PATRIC; fig|176280.10.peg.1027; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_1_9; -.
DR   OMA; RGPHDLI; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000001411; 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..262
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_0000154255"
SQ   SEQUENCE   262 AA;  30123 MW;  258ABAF1C0A02287 CRC64;
     MTILNEIIEY KKTLLERKYY DKKLEILQDN GNVKRRKLID SLNYDRTLSV IAEIKSKSPS
     VPQLPQRDLV QQVKDYQKYG ANAISILTDE KYFGGSFERL NQLSKITSLP VLCKDFIIDK
     IQIDVAKRAG ASIILLIVNI LSDDQLKELY SYAINHNLEV LVEVHTIREL ERAHQINPKI
     IGVNNRDLKR FETDVLHTNK LLKFKKSNCC YISESGIHTK EDVEKIVDSN IDGLLVGEAL
     MKTNDLSQFL PSLKLKKNLY DS