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TRPC_BACCR
ID   TRPC_BACCR              Reviewed;         253 AA.
AC   Q81GG7;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=BC_1235;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08220.1; -; Genomic_DNA.
DR   RefSeq; NP_831019.1; NC_004722.1.
DR   RefSeq; WP_000536703.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81GG7; -.
DR   SMR; Q81GG7; -.
DR   STRING; 226900.BC_1235; -.
DR   EnsemblBacteria; AAP08220; AAP08220; BC_1235.
DR   GeneID; 67505953; -.
DR   KEGG; bce:BC1235; -.
DR   PATRIC; fig|226900.8.peg.1206; -.
DR   HOGENOM; CLU_034247_2_0_9; -.
DR   OMA; RGPHDLI; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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..253
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /id="PRO_0000154209"
SQ   SEQUENCE   253 AA;  28290 MW;  2519649E1A8081C8 CRC64;
     MGTILDKIVE QKKKEVAELY EIYTPVKTKR KTQSLVEALQ QFTVIAEVKR ASPSKGDINL
     HVDVRKQVGT YEKCGAGAVS VLTDGQFFKG SFHDLQTARE ESNIPLLCKD FIIDKIQIDR
     AYEAGADIIL LIVAALTKEK LKELYSYVLE KGLEAIVEVH DEQELETAIV LNPHVIGINN
     RNLKTFEVDL SQTEKLGKRL NEEKLLWISE SGIHSKEDII RVKRAGAKGV LVGEALMTSS
     SISSFFEDCK VNI
 
 
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