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Database: UniProt
Entry: A0A0C4YGN1_9BURK
LinkDB: A0A0C4YGN1_9BURK
Original site: A0A0C4YGN1_9BURK 
ID   A0A0C4YGN1_9BURK        Unreviewed;       267 AA.
AC   A0A0C4YGN1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ECO:0000313|EMBL:QOT76065.1};
GN   ORFNames=F7R26_018230 {ECO:0000313|EMBL:QOT76065.1}, RR42_m3729
GN   {ECO:0000313|EMBL:AJG21089.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG21089.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG21089.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG21089.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT   Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
RN   [2] {ECO:0000313|EMBL:QOT76065.1, ECO:0000313|Proteomes:UP000397656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 49340 {ECO:0000313|Proteomes:UP000397656}, and DSM 11853
RC   {ECO:0000313|EMBL:QOT76065.1};
RA   Salva-Serra F., Donoso R.A., Cho K.H., Yoo J.A., Lee K., Yoon S.-H.,
RA   Perez-Pantoja D., Moore E.R.B.;
RT   "Complete genome sequence of Cupriavidus basilensis CCUG 49340T.";
RL   Submitted (OCT-2020) 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}.
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DR   EMBL; CP010536; AJG21089.1; -; Genomic_DNA.
DR   EMBL; CP062803; QOT76065.1; -; Genomic_DNA.
DR   RefSeq; WP_043349935.1; NZ_SUQM01000079.1.
DR   AlphaFoldDB; A0A0C4YGN1; -.
DR   STRING; 68895.RR42_m3729; -.
DR   KEGG; cbw:RR42_m3729; -.
DR   OrthoDB; 9804217at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000031843; Chromosome main.
DR   Proteomes; UP000397656; Chromosome 1.
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_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   Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          5..262
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
SQ   SEQUENCE   267 AA;  28995 MW;  735E38A677DFDB01 CRC64;
     MSDILQKILA VKADEVNAAR KKRDLPSLRA EAESLRAEPG LAPRGFERAL REKIAAGNAG
     VIAEVKKASP SKGVLRANFV PEAIAESYAT HGAACLSVLT DVNFFQGHAE FLKRARGACP
     LPALRKDFMI DLYQVYEARC WGADAILLIV SALDPGLMAE LEACAHELGM DVLVEVHGGE
     ELDAALRLKT PLLGVNNRNL RTFEVSLDNT LDLLPRIPDD RLVVTESGII GPDDVHRMRD
     ANVHAFLVGE AFMRAPDPGV ELARLFA
//
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