ID   TRPC_SALRD              Reviewed;         270 AA.
AC   Q2S1Z5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=SRU_1667;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC44256.1; -; Genomic_DNA.
DR   RefSeq; WP_011404412.1; NC_007677.1.
DR   RefSeq; YP_445786.1; NC_007677.1.
DR   AlphaFoldDB; Q2S1Z5; -.
DR   SMR; Q2S1Z5; -.
DR   STRING; 309807.SRU_1667; -.
DR   EnsemblBacteria; ABC44256; ABC44256; SRU_1667.
DR   GeneID; 61496292; -.
DR   KEGG; sru:SRU_1667; -.
DR   PATRIC; fig|309807.25.peg.1729; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_0_10; -.
DR   OMA; RGPHDLI; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000008674; 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..270
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_1000198786"
SQ   SEQUENCE   270 AA;  29779 MW;  942D29554DF98DDA CRC64;
     MSILDDIIDD TRELVEQRKQ ETPTSELKER PFYDEREPLS LAEALKERGL SFIAEVKKAS
     PSKGVIRDPF DPAAIAQQYA EHDAAAISVL TEPLHFEGAL EHMAWIRAHV PETPLLRKDF
     IIDPYQLVEA RAVGADAVLL IATALDPGQL AELHAAATEL GLSCLVEVYE EEDLDKIDWE
     QVSVLGVNNR DLHTFEVDLD NSLRIFDQTP KGVGRVAESG LSDPETLVRL RKAGVNGVLI
     GEHLMRAEHP GEALSRLRAE GKKIAAQQAG