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Database: UniProt
Entry: W0AL47_9SPHN
LinkDB: W0AL47_9SPHN
Original site: W0AL47_9SPHN 
ID   W0AL47_9SPHN            Unreviewed;       262 AA.
AC   W0AL47;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=NX02_27085 {ECO:0000313|EMBL:AHE57003.1};
OS   Sphingomonas sanxanigenens DSM 19645 = NX02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE57003.1, ECO:0000313|Proteomes:UP000018851};
RN   [1] {ECO:0000313|EMBL:AHE57003.1, ECO:0000313|Proteomes:UP000018851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NX02 {ECO:0000313|EMBL:AHE57003.1,
RC   ECO:0000313|Proteomes:UP000018851};
RA   Ma T., Huang H., Wu M., Li X., Li G.;
RT   "Completed genome of Sphingomonas sanxanigenens NX02.";
RL   Submitted (JUL-2013) 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; CP006644; AHE57003.1; -; Genomic_DNA.
DR   RefSeq; WP_025295101.1; NZ_CP006644.1.
DR   AlphaFoldDB; W0AL47; -.
DR   STRING; 1123269.NX02_27085; -.
DR   KEGG; ssan:NX02_27085; -.
DR   PATRIC; fig|1123269.5.peg.5314; -.
DR   eggNOG; COG0134; Bacteria.
DR   HOGENOM; CLU_034247_2_0_5; -.
DR   OrthoDB; 9804217at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000018851; 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:UP000018851};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          5..259
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
SQ   SEQUENCE   262 AA;  28530 MW;  F921C4C052207EE8 CRC64;
     MTDMLAEICA TKRLEVDRRK AHTPFADLEA RARAATPPRG FRAALDAKAA TGHALIAEVK
     KASPSKGLIR EHFDPHAHAL AYQSGGAACL SVLTDEPYFM GHDDYLVAAR AAVSLPCLRK
     DFLVDPWQVT EARALGADCI LIIAAALDDA QMADIEAEAI RWGMDALVEV HDADELERAL
     KLRSRLIGVN NRDLRDFSIS FERTYELVDR APAGCTFVAE SGLRDKADLD AMAARGVRCF
     LVGEALMRQD DVEAATRALI VG
//
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