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Database: UniProt
Entry: A0A366HT15_9BACT
LinkDB: A0A366HT15_9BACT
Original site: A0A366HT15_9BACT 
ID   A0A366HT15_9BACT        Unreviewed;       264 AA.
AC   A0A366HT15;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00134};
DE            Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE            EC=4.1.1.48 {ECO:0000256|HAMAP-Rule:MF_00134};
GN   Name=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN   ORFNames=DES53_102219 {ECO:0000313|EMBL:RBP45837.1};
OS   Roseimicrobium gellanilyticum.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobiaceae; Roseimicrobium.
OX   NCBI_TaxID=748857 {ECO:0000313|EMBL:RBP45837.1, ECO:0000313|Proteomes:UP000253426};
RN   [1] {ECO:0000313|EMBL:RBP45837.1, ECO:0000313|Proteomes:UP000253426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25532 {ECO:0000313|EMBL:RBP45837.1,
RC   ECO:0000313|Proteomes:UP000253426};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001633, ECO:0000256|HAMAP-
CC         Rule:MF_00134};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC       ECO:0000256|HAMAP-Rule:MF_00134}.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00134}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RBP45837.1}.
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DR   EMBL; QNRR01000002; RBP45837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366HT15; -.
DR   OrthoDB; 9804217at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000253426; Unassembled WGS sequence.
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; Aldolase class I; 1.
DR   HAMAP; MF_00134_A; IGPS_A; 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:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00134};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00134};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00134};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00134};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          4..254
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
SQ   SEQUENCE   264 AA;  29369 MW;  82DC3FD2D1776BE7 CRC64;
     MNKLDEIIAH KHTEVQRLLP RMEKLRAAAA GRNDFRSLYD ALRADPGHMG LIAEVKKASP
     SAGVIQPDFD YLTIARTYEK GGANALSVLT DEKYFQGKLE YMTTIRNEVS IPVLRKDFII
     HEAQIFEAVV AGADAILLIV AALKQDQLEH LLEVAHTFQL DVLMEVHDLP ELERALATNV
     RILGINNRNL KSFTVDLATT EALVEEVPDD VVLVSESGIK SVEDAQRLAD AGADALLVGE
     TLMRHERPMD MARALRVERV IVEK
//
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