TRPC_PROM3
ID TRPC_PROM3 Reviewed; 301 AA.
AC A2CB59;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-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=P9303_19771;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM78719.1; -; Genomic_DNA.
DR AlphaFoldDB; A2CB59; -.
DR SMR; A2CB59; -.
DR STRING; 59922.P9303_19771; -.
DR EnsemblBacteria; ABM78719; ABM78719; P9303_19771.
DR KEGG; pmf:P9303_19771; -.
DR HOGENOM; CLU_034247_2_0_3; -.
DR OMA; RGPHDLI; -.
DR BioCyc; PMAR59922:G1G80-1717-MON; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000002274; 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..301
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000018521"
SQ SEQUENCE 301 AA; 32800 MW; B0CD083F8D280E05 CRC64;
MEIRRRPPNP SVKVAHLQYA IPHADAEPRH ILEKIVWEKD REVETARQRV PLETLKSQIA
DLPIPRDFIA ALRQASVAPA VIAEVKKASP SQGVIRADFD PVLIANAYAE GGASCLSVLT
DKSFFQGGFE VLVEVRQTVG LPLLCKDFIL TPYQLYQARA AGADAALLIM AILSDQDLTY
LSKVANSLGL TVLVEVHDAE ELERVLNLGG FPLIGINNRD LTTFETDLET TETLSKQFAT
RLKQQGVLLV SESGLFNRAD LDRVQAVGAE AVLVGEALMR QSDVCAGLKQ LMIGDEGTSN
S