TRPC_POLAQ
ID TRPC_POLAQ Reviewed; 267 AA.
AC A4SV52;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Pnuc_0145;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP33366.1; -; Genomic_DNA.
DR RefSeq; WP_011901991.1; NC_009379.1.
DR AlphaFoldDB; A4SV52; -.
DR SMR; A4SV52; -.
DR STRING; 312153.Pnuc_0145; -.
DR PRIDE; A4SV52; -.
DR EnsemblBacteria; ABP33366; ABP33366; Pnuc_0145.
DR GeneID; 31480494; -.
DR KEGG; pnu:Pnuc_0145; -.
DR eggNOG; COG0134; Bacteria.
DR HOGENOM; CLU_034247_2_0_4; -.
DR OMA; RGPHDLI; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000231; 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..267
FT /note="Indole-3-glycerol phosphate synthase"
FT /id="PRO_1000076422"
SQ SEQUENCE 267 AA; 29206 MW; 366B12EB3F3D58A8 CRC64;
MSDILDKIVA TKKIEVAHNS SKISLGNHRE QAEANNQSNL LKPRGFIQAI ERKISAGKAG
VITEVKKASP SKGILRENFI SAEIAQSYEK HGAACLSVLT DSDYFQGCNA YLQEARAACQ
IPVLRKDFTI DPYQIYEARA IGADAILLIV ACLELNQMME LEACAHELGL DVLVEVHNAP
ELEQALELKT PLLGINNRNL KTFEVSLQTT LSLLSSVPKN KTLVTESGIL SRADVELMRK
NQINAFLVGE AFMRAPDPGT ALSELFA