TRPC_STRM5
ID TRPC_STRM5 Reviewed; 264 AA.
AC B4SLE8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00134};
DE Short=IGPS {ECO:0000255|HAMAP-Rule:MF_00134};
DE EC=4.1.1.48 {ECO:0000255|HAMAP-Rule:MF_00134};
GN Name=trpC {ECO:0000255|HAMAP-Rule:MF_00134}; OrderedLocusNames=Smal_3718;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) 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:0000255|HAMAP-Rule:MF_00134};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00134}.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000255|HAMAP-
CC Rule:MF_00134}.
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DR EMBL; CP001111; ACF53417.1; -; Genomic_DNA.
DR RefSeq; WP_012512312.1; NC_011071.1.
DR AlphaFoldDB; B4SLE8; -.
DR SMR; B4SLE8; -.
DR STRING; 391008.Smal_3718; -.
DR EnsemblBacteria; ACF53417; ACF53417; Smal_3718.
DR KEGG; smt:Smal_3718; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_6; -.
DR OMA; RGPHDLI; -.
DR OrthoDB; 1789381at2; -.
DR BioCyc; SMAL391008:SMAL_RS18885-MON; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000001867; 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; -; 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; PTHR22854; 1.
DR Pfam; PF00218; IGPS; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW Lyase; Tryptophan biosynthesis.
FT CHAIN 1..264
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000095895"
SQ SEQUENCE 264 AA; 28677 MW; 544486158B6C470D CRC64;
MSDILQTILA RKAEEVAQRR AQRPLEDLQV AVASAPPVRG FVRALQAAVA NGDPAVIAEV
KKASPSKGVI RPDFRPADIA VSYEFGGASC LSVLTDVDFF QGADAYLQQA RDACTLPVLR
KDFVIDAYQV YEARVLGADC ILLIVAALDD TQLATLSELA MSLGMDVLVE VHDIDELERA
LQVPAPMIGI NNRNLRTFEV SLQTTLDMQK AVPRDRLLVT ESGILGPQDV ALMRDAGIHS
FLVGEAFMRV EEPGEGLRQL FFAA