ID   TRPC_PRIM1              Reviewed;         255 AA.
AC   P70937; D5DRF2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Indole-3-glycerol phosphate synthase;
DE            Short=IGPS;
DE            EC=4.1.1.48;
GN   Name=trpC; OrderedLocusNames=BMQ_4321;
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=545693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Jablonski L.M., Vary P.S., Hudspeth D.S.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
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DR   EMBL; U67986; AAB07592.1; -; Genomic_DNA.
DR   EMBL; CP001983; ADE71331.1; -; Genomic_DNA.
DR   RefSeq; WP_013059004.1; NC_014019.1.
DR   AlphaFoldDB; P70937; -.
DR   SMR; P70937; -.
DR   STRING; 545693.BMQ_4321; -.
DR   EnsemblBacteria; ADE71331; ADE71331; BMQ_4321.
DR   GeneID; 64145973; -.
DR   KEGG; bmq:BMQ_4321; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_0_9; -.
DR   OMA; RGPHDLI; -.
DR   OrthoDB; 1789381at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000935; 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_0000154211"
SQ   SEQUENCE   255 AA;  28689 MW;  BB2B4A21114B6430 CRC64;
     MLNKIIETKK EEIQNLQLPE QQNVAKRSFL DALSNPNREL ALIAEVKKAS PSKGLIKENF
     QPVEIAKAYE KGKADALSVL TDQHYFQGHR TFLSDIKQHV SVPVLRKDFI IDSIQVEESA
     RIGADAILLI GEALEPLKLQ ELYLQAAEKE LDCLVEVHSL ETLEKLLAVF TPKIIGINNR
     NLHTFETSLQ QTKEIAKHVP KDQLLVSESG IYLYDDVSYV KEAGAKAILV GESLMRQDNQ
     TKAIEKLFGE SEYAH