TRPC_PSEPF
ID TRPC_PSEPF Reviewed; 278 AA.
AC Q3K5V4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=Pfl01_5113;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA76850.1; -; Genomic_DNA.
DR RefSeq; WP_011336192.1; NC_007492.2.
DR AlphaFoldDB; Q3K5V4; -.
DR SMR; Q3K5V4; -.
DR STRING; 205922.Pfl01_5113; -.
DR PRIDE; Q3K5V4; -.
DR EnsemblBacteria; ABA76850; ABA76850; Pfl01_5113.
DR KEGG; pfo:Pfl01_5113; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_6; -.
DR OMA; RGPHDLI; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000002704; 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..278
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000018536"
SQ SEQUENCE 278 AA; 30294 MW; 54072D087D8880A8 CRC64;
MSVPTVLENI LARKFQEVAE RSARVSLSEL ESLAKAADAP RGFAQALLAQ AKKKQPAVIA
EIKKASPSKG VIRENFVPAD IAKSYEKGGA TCLSVLTDID YFQGADAYLQ QARVACSLPV
IRKDFMIDPY QIVEARALGA DCVLLIVSAL DDVKMAELAS VAKDVGLDVL VEVHDGDELE
RALKTLDTPL VGVNNRNLHT FDVSLETTLD LLPRIPRDRL VITESGILNR ADVELMEISD
VYAFLVGEAF MRAENPGIEL QRLFFPERGV PVSGSTLD