ID   TRPC_DICNV              Reviewed;         267 AA.
AC   A5EVG3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=DNO_0585;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(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; CP000513; ABQ13361.1; -; Genomic_DNA.
DR   RefSeq; WP_012030919.1; NC_009446.1.
DR   AlphaFoldDB; A5EVG3; -.
DR   SMR; A5EVG3; -.
DR   STRING; 246195.DNO_0585; -.
DR   PRIDE; A5EVG3; -.
DR   EnsemblBacteria; ABQ13361; ABQ13361; DNO_0585.
DR   KEGG; dno:DNO_0585; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_0_6; -.
DR   OMA; RGPHDLI; -.
DR   OrthoDB; 1789381at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000248; 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; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Lyase; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..267
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_1000057872"
SQ   SEQUENCE   267 AA;  29716 MW;  170AC8239BB69CCD CRC64;
     MTKILDDIVA YKQQEIAALK QQKTEASLIA ELETLTDAPR GFMRALRDCR DRGGVAVVAE
     IKRASPNQGL LREQFMPELL AQECVQYGAS CLSVFTDTHF FYGDVAYLSA VKKAVPVPVL
     RKDFIISRYQ ILESRLLGVD CILLIVAILT DEQLQEFVVL AHDLGMDVLI EIHDENDLKR
     ALNVPVRTLA INNRNPEDFN ASLEKSAQLR QQLPKDYFVI SESGINTHAD VVYLLNCGLD
     AVLIGGALMS AEFAGEALHH LIYGKED