ID A0A1Q3L2C2_9MICO Unreviewed; 267 AA.
AC A0A1Q3L2C2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN ORFNames=BGN97_06535 {ECO:0000313|EMBL:OJU39267.1};
OS Microbacterium sp. 69-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1895783 {ECO:0000313|EMBL:OJU39267.1, ECO:0000313|Proteomes:UP000185697};
RN [1] {ECO:0000313|EMBL:OJU39267.1, ECO:0000313|Proteomes:UP000185697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69-10 {ECO:0000313|EMBL:OJU39267.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJU39267.1}.
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DR EMBL; MKRT01000028; OJU39267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3L2C2; -.
DR STRING; 1895783.BGN97_06535; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000185697; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 8..246
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
SQ SEQUENCE 267 AA; 28111 MW; C83D9DC931C41FA7 CRC64;
MVLADLTAGA VQDAERRAAT RPLADVEREA LARPAARDAL AALAPADRVK IIAEVKRASP
SRGALAEIPD PALQASLYEQ GGASAISVLT EERRFGGSLA DLEAVTARVN LPVLRKDFIA
TPYQVLEARA AGADLALLIV AGLDVKTLGE LYALIRELGM TPLIETHSAE ELEVAIDLGA
ELIGVNARNL KTLELDRDLF ASLSERIPDT AIRVAESAVL APEDVRRYRE AGADVVLIGE
ALVTGDPVAT LNAFLAAGDL PVRGGEE
//