ID   TRPC_PROMS              Reviewed;         295 AA.
AC   A2BSL8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=A9601_14961;
OS   Prochlorococcus marinus (strain AS9601).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=146891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS9601;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000551; ABM70779.1; -; Genomic_DNA.
DR   RefSeq; WP_011818915.1; NC_008816.1.
DR   AlphaFoldDB; A2BSL8; -.
DR   SMR; A2BSL8; -.
DR   STRING; 146891.A9601_14961; -.
DR   EnsemblBacteria; ABM70779; ABM70779; A9601_14961.
DR   KEGG; pmb:A9601_14961; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_1_0_3; -.
DR   OMA; RGPHDLI; -.
DR   OrthoDB; 1789381at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000002590; 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..295
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_1000018527"
SQ   SEQUENCE   295 AA;  33628 MW;  9F6CACF18B359BA1 CRC64;
     MEIRRRPPNP TVRVENLEYA VPHREAQAKN ILEEIVWHKD IEIKNFKKIV SLEDLIKKIE
     NLPTPKDFYK NILESKIKPG VIAEIKKASP SKGVIRKDFN PENIAICYEG LGASCISVLT
     DKKFFQGSYE ILETVRKSTN LPLLCKDFII SAYQIYKARV SGADAILLIA AILSDDDLIY
     LKKIADNLKM SVLVEVHNSY ELERILKLKS FNLIGINNRD LKTFKTDLKT SKELMNTYAD
     IFLKQNIIPI SESGINCAED LESLRSIGIM GVLIGETFMR ETDIEQSFKK LFNSI