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Database: UniProt
Entry: S3V114_9LEPT
LinkDB: S3V114_9LEPT
Original site: S3V114_9LEPT 
ID   S3V114_9LEPT            Unreviewed;       249 AA.
AC   S3V114;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE            EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN   Name=trpC {ECO:0000313|EMBL:EPG74314.1};
GN   ORFNames=LEP1GSC058_2388 {ECO:0000313|EMBL:EPG74314.1};
OS   Leptospira fainei serovar Hurstbridge str. BUT 6.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193011 {ECO:0000313|EMBL:EPG74314.1, ECO:0000313|Proteomes:UP000014540};
RN   [1] {ECO:0000313|EMBL:EPG74314.1, ECO:0000313|Proteomes:UP000014540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUT 6 {ECO:0000313|EMBL:EPG74314.1,
RC   ECO:0000313|Proteomes:UP000014540};
RA   Harkins D.M., Durkin A.S., Selengut J.D., Sanka R., DePew J., Purushe J.,
RA   Ahmed A., van der Linden H., Goris M.G.A., Hartskeerl R.A., Vinetz J.M.,
RA   Sutton G.G., Nelson W.C., Fouts D.E.;
RL   Submitted (APR-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};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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:EPG74314.1}.
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DR   EMBL; AKWZ02000010; EPG74314.1; -; Genomic_DNA.
DR   RefSeq; WP_016550770.1; NZ_AKWZ02000010.1.
DR   AlphaFoldDB; S3V114; -.
DR   STRING; 1193011.LEP1GSC058_2388; -.
DR   OrthoDB; 9804217at2; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000014540; Unassembled WGS sequence.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00331; IGPS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EPG74314.1};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   DOMAIN          17..245
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
SQ   SEQUENCE   249 AA;  27892 MW;  FE0D1A31A2E94965 CRC64;
     MGLHRVLRDI LETKKRELET IPEYTPVKYS GPSLWQSLRS RKFSIIAECK RKSPSAGTIR
     ETYEPTQIAK VYEECGASGI SVLTDTDYFG GSLEHLRQVS EKVNIPVLRK DFIIDERQVI
     EAREYGAGAI LLIVRILDPD TLKNLILAAT KLGMGVLTEI HTEEEAEIAR DAGANIVGIN
     TRDLDDFSIH KDLVPKVANK LSPNIVKVGE SGIKSKQDLD AFRPYVDAAL IGTYFMEKSD
     IRTAWLELF
//
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