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Database: UniProt
Entry: L0IBF5_HALRX
LinkDB: L0IBF5_HALRX
Original site: L0IBF5_HALRX 
ID   L0IBF5_HALRX            Unreviewed;       275 AA.
AC   L0IBF5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|ARBA:ARBA00018080, ECO:0000256|HAMAP-Rule:MF_00134};
DE            Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE            EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362, ECO:0000256|HAMAP-Rule:MF_00134};
GN   Name=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN   OrderedLocusNames=Halru_2300 {ECO:0000313|EMBL:AGB16885.1};
OS   Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halovivax.
OX   NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB16885.1, ECO:0000313|Proteomes:UP000010846};
RN   [1] {ECO:0000313|Proteomes:UP000010846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18193 / JCM 13892 / XH-70
RC   {ECO:0000313|Proteomes:UP000010846};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Halovivax ruber XH-70.";
RL   Submitted (SEP-2011) 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|ARBA:ARBA00008737,
CC       ECO:0000256|HAMAP-Rule:MF_00134}.
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DR   EMBL; CP003050; AGB16885.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0IBF5; -.
DR   STRING; 797302.Halru_2300; -.
DR   KEGG; hru:Halru_2300; -.
DR   eggNOG; arCOG01088; Archaea.
DR   HOGENOM; CLU_034247_0_1_2; -.
DR   OrthoDB; 15223at2157; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000010846; 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_A; IGPS_A; 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   NCBIfam; NF041303; Indglycph_syn_Halo_TrpC; 1.
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:UP000010846};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          26..254
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
SQ   SEQUENCE   275 AA;  29156 MW;  F919D2CA3B0DA11E CRC64;
     MNDKGLDPAV RSILEAARDR SGRGDERLSV HARSLAAAIE RAESDGRVPI VAEVKPTSPT
     TDGVRTDDPV ELAQQMVDGG ATAISVLTEP DHFDGSTAAL ARVREAVSVP VLRKDFVVRE
     EQLDAVEADL VLLIARFVDE LDELVSAALD RGLQPIVEVH DRAELRRALA TETAVVGINN
     RDLASLEVDL TTVERVAAVE DPSLRQALDD VTLVAESGVS TPADVRRMRE AGADALLVGS
     AIMDGDVAAN TRALVNAERA VETDDADTAS EVDAA
//
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