ID A0A2S5X3X0_9MICO Unreviewed; 257 AA.
AC A0A2S5X3X0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN ORFNames=C5C17_09975 {ECO:0000313|EMBL:PPG39143.1};
OS Pseudoclavibacter sp. RFBA6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pseudoclavibacter.
OX NCBI_TaxID=2080573 {ECO:0000313|EMBL:PPG39143.1, ECO:0000313|Proteomes:UP000237697};
RN [1] {ECO:0000313|EMBL:PPG39143.1, ECO:0000313|Proteomes:UP000237697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RFBA6 {ECO:0000313|EMBL:PPG39143.1,
RC ECO:0000313|Proteomes:UP000237697};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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:PPG39143.1}.
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DR EMBL; PSUA01000012; PPG39143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5X3X0; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000237697; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000237697};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 2..252
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
SQ SEQUENCE 257 AA; 27613 MW; C90E3B8FB88AD548 CRC64;
MLESLYHGAL EDAAERRERT PARALEARIA DVAPALDAYS ALARSERVNI IAEVKRASPS
RGRLADIPDP AVLAASYERG GAAAISVLTE QRKFLGSLDD LRAVRDTVAV PVLRKEFIAE
EYQLLEARAC GADLALLIVA GLDQSTLVRL AEFTEQLGMT ALVEAHSKDE LLRGLDAGAR
ILGVNARNLA TFELHPELFG ELAPLYPSDV VKVAESAVLE PAHVRRYRDA GADAVLIGEA
LVTGGDPETT LETFHLA
//
