ID E8NFN7_MICTS Unreviewed; 258 AA.
AC E8NFN7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:BAJ76519.1};
GN OrderedLocusNames=MTES_3555 {ECO:0000313|EMBL:BAJ76519.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ76519.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ76519.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ76519.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-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};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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DR EMBL; AP012052; BAJ76519.1; -; Genomic_DNA.
DR RefSeq; WP_013586641.1; NC_015125.1.
DR AlphaFoldDB; E8NFN7; -.
DR STRING; 979556.MTES_3555; -.
DR KEGG; mts:MTES_3555; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_0_0_11; -.
DR OrthoDB; 9804217at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000008975; Chromosome.
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 7..245
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 258 AA; 27210 MW; AB47B8A48F8311B0 CRC64;
MLADLTAGAV EDAEKRAETR PLAEVERDAL AQTPPRDALA MLAPADRVKI IAEVKRASPS
RGDLASIPDP ARQARLYEEG GASAISVLTE GRKFKGSLAD LEAVRAAVSV PVLRKDFIAT
PYQVLEARAS AADLVLLIVA ALDQKTLTEL YGLVTDLGMT ALVETHSADE LERATDLGAK
LIGVNARNLS TFELDRDLFG SLADRFPADA VKIAESAVLA PADVAHYRAA GADVVLVGEA
LVTGDPVATL RAFLQETS
//
