TRPC_SYNE7
ID TRPC_SYNE7 Reviewed; 295 AA.
AC Q8KPR4; Q31NZ2;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-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};
GN OrderedLocusNames=Synpcc7942_1197; ORFNames=see0030;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S.,
RA Gonzalez A., Salinas I., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 7G3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM82705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY120853; AAM82705.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000100; ABB57227.1; -; Genomic_DNA.
DR RefSeq; WP_011242666.1; NC_007604.1.
DR AlphaFoldDB; Q8KPR4; -.
DR SMR; Q8KPR4; -.
DR STRING; 1140.Synpcc7942_1197; -.
DR PRIDE; Q8KPR4; -.
DR EnsemblBacteria; ABB57227; ABB57227; Synpcc7942_1197.
DR KEGG; syf:Synpcc7942_1197; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_1_0_3; -.
DR OMA; RGPHDLI; -.
DR OrthoDB; 1789381at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1197-MON; -.
DR UniPathway; UPA00035; UER00043.
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..295
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_0000154264"
SQ SEQUENCE 295 AA; 32402 MW; 3E215B7318F6A052 CRC64;
MEVRRRPPNP AVHVASLTYQ VKVPGSSPSN ILEEIVWYKE REVNAWREQL PLQQLQNQVR
GLTQTPRDFL AALRQAPTRP AVIAEVKKAS PSKGVLREDF DPVAIAQAYA ANGAACISVL
TDEKFFQGGF ENLQRVRAAV DVPLLCKDFV IYPYQIYKAR LLGADAVLLI AAILSDADLR
YFLKIAHSLG LNALVEVHSL PELERVLALD DLRLVGINNR NLKTFVTDLA VTEHLAAQCR
DRDLLLVSES GLFTGADLDR VTQAGAQAVL IGESLVKQPD PGLALQQLVG DRPSA