ID B4S5E9_PROA2 Unreviewed; 259 AA.
AC B4S5E9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 OrderedLocusNames=Paes_0490 {ECO:0000313|EMBL:ACF45546.1};
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF45546.1, ECO:0000313|Proteomes:UP000002725};
RN [1] {ECO:0000313|EMBL:ACF45546.1, ECO:0000313|Proteomes:UP000002725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL Submitted (JUN-2008) 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; CP001108; ACF45546.1; -; Genomic_DNA.
DR RefSeq; WP_012505083.1; NC_011059.1.
DR AlphaFoldDB; B4S5E9; -.
DR STRING; 290512.Paes_0490; -.
DR KEGG; paa:Paes_0490; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_10; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000002725; 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; 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:UP000002725};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00134}.
FT DOMAIN 5..249
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
SQ SEQUENCE 259 AA; 29029 MW; 405CB1EF4B71BBEE CRC64;
MTTYLTRILE FKAGEVRDLK QRSPERLYRE KVAELPPVRD FYGALRRAPE SPINLIAEVK
KASPSRGILV EDFHPLDIAR RYAELGASAF SVLTDREFFQ GSNDYLQLVA SSCDIPVLRK
DFIIDESQIF EARLIGADAI LLIVAALEPA QLGEYLSLAH ELGLAVLVEV HDEHELEHAL
EQGSRMIGVN NRDLRDFTFS LDTSLRLRPK MPSGIIAVAE SGLKRSSDVM MMQEASFDAV
LIGEGLLGEE LQGFTWKRI
//
