TRPC_DESRM
ID TRPC_DESRM Reviewed; 265 AA.
AC A4J147;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Dred_0251;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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; CP000612; ABO48800.1; -; Genomic_DNA.
DR RefSeq; WP_011876638.1; NC_009253.1.
DR AlphaFoldDB; A4J147; -.
DR SMR; A4J147; -.
DR STRING; 349161.Dred_0251; -.
DR EnsemblBacteria; ABO48800; ABO48800; Dred_0251.
DR KEGG; drm:Dred_0251; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_9; -.
DR OMA; RGPHDLI; -.
DR OrthoDB; 1789381at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000001556; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..265
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000071434"
SQ SEQUENCE 265 AA; 29314 MW; F1563557FE17405A CRC64;
MILEKIKEKK REEIRQLLLT ANVAHMKKKI LELPPARDFR KALYNQGQVS LIAEIKKASP
SKGLLCPNFD HRQLAHIYQS NGAAALSVLT DENFFLGKLT YLEEIKQQSS LPLLRKDFIL
DPVQLYQSRL AGADAVLLIA GLLTPGELSQ LFLLCREIGM QALVEVHTQE ELQRVLTTDA
KLIGINNRDL STFQTNLATT AKLLEQVQIE DITIVSESGI AQKEDIKFLK SLGVHGVLVG
EALVTAQDIA KKVQEIVVAG GRGEA