ID TRPC_MYCLE Reviewed; 272 AA.
AC Q9X7C7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Indole-3-glycerol phosphate synthase;
DE Short=IGPS;
DE EC=4.1.1.48;
GN Name=trpC; OrderedLocusNames=ML1271; ORFNames=MLCB1610.33;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
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DR EMBL; AL049913; CAB43179.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31652.1; -; Genomic_DNA.
DR PIR; T45256; T45256.
DR RefSeq; NP_301916.1; NC_002677.1.
DR RefSeq; WP_010908237.1; NC_002677.1.
DR AlphaFoldDB; Q9X7C7; -.
DR SMR; Q9X7C7; -.
DR STRING; 272631.gene:17575103; -.
DR KEGG; mle:ML1271; -.
DR PATRIC; fig|272631.5.peg.2335; -.
DR Leproma; ML1271; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_0_0_11; -.
DR OrthoDB; 9804217at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000806; 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; Aldolase class I; 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: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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW Lyase; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..272
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_0000154233"
SQ SEQUENCE 272 AA; 28145 MW; DA5596D8D1D0DC59 CRC64;
MCPATVLDSI LKGVRADVAA REACISLSEI KAAAAAAPAP LDAMAALREP GIGVIAEVKR
ASPSVGSLAT IADPAKLAQA YEDGGARIIS VLTEERRFNG SLDDLDAVRA AVSVPVLRKD
FVVQPYQIHE ARAHGADMLL LIVAALDQSA LMSMLDRTES LGMIALVEVR TEQEADRALK
AGAKVIGVNA RDLMTLEVDR DCFSRIAPGL PSNVIRIAES GVRGPADLLA YAGAGADAVL
VGEGLVKSGD PRAAVADLVT AGTHPSCPKP AR
//
