ID TRPC_PSEAE Reviewed; 278 AA. AC P20577; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 10-JUN-2026, entry version 140. DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; GN Name=trpC; OrderedLocusNames=PA0651; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2105306; DOI=10.1128/jb.172.2.853-866.1990; RA Essar D.W., Eberly L., Han C.Y., Crawford I.P.; RT "DNA sequences and characterization of four early genes of the tryptophan RT pathway in Pseudomonas aeruginosa."; RL J. Bacteriol. 172:853-866(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-278. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=8002577; DOI=10.1128/jb.176.24.7532-7542.1994; RA West S.E.H., Sample A.K., Runyen-Janecky L.J.; RT "The vfr gene product, required for Pseudomonas aeruginosa exotoxin A and RT protease production, belongs to the cyclic AMP receptor protein family."; RL J. Bacteriol. 176:7532-7542(1994). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M33814; AAA25825.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04040.1; -; Genomic_DNA. DR PIR; C35114; C35114. DR RefSeq; NP_249342.1; NC_002516.2. DR RefSeq; WP_003113174.1; NC_002516.2. DR PDB; 6Y88; X-ray; 2.10 A; A/B/C/D/E/F/H=1-278, G=25-278. DR AlphaFoldDB; P20577; -. DR SMR; P20577; -. DR FunCoup; P20577; 430. DR STRING; 208964.PA0651; -. DR PaxDb; 208964-PA0651; -. DR GeneID; 882120; -. DR KEGG; pae:PA0651; -. DR PATRIC; fig|208964.12.peg.682; -. DR PseudoCAP; PA0651; -. DR HOGENOM; CLU_034247_2_0_6; -. DR InParanoid; P20577; -. DR OrthoDB; 9804217at2; -. DR PhylomeDB; P20577; -. DR BioCyc; PAER208964:G1FZ6-656-MONOMER; -. DR BRENDA; 4.1.1.48; 5087. DR SABIO-RK; P20577; -. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000002438; Chromosome. DR AbasyAtlas; P20577; -. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IDA:PseudoCAP. DR GO; GO:0000162; P:L-tryptophan biosynthetic process; IMP:PseudoCAP. DR CDD; cd00331; IGPS; 1. DR FunFam; 3.20.20.70:FF:000024; Indole-3-glycerol phosphate synthase; 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 NCBIfam; NF001370; PRK00278.1-2; 1. DR NCBIfam; NF001373; PRK00278.1-6; 1. DR NCBIfam; NF001377; PRK00278.2-4; 1. 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. DR PDBsum; 6Y88; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Decarboxylase; Lyase; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..278 FT /note="Indole-3-glycerol phosphate synthase" FT /id="PRO_0000154238" FT HELIX 5..24 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 27..36 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 43..51 FT /evidence="ECO:0007829|PDB:6Y88" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6Y88" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 78..88 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:6Y88" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 106..115 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 129..137 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 152..164 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 168..175 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 189..194 FT /evidence="ECO:0007829|PDB:6Y88" FT TURN 198..200 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 219..225 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 230..238 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:6Y88" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:6Y88" FT HELIX 256..264 FT /evidence="ECO:0007829|PDB:6Y88" SQ SEQUENCE 278 AA; 30347 MW; 478FEF45378B55F8 CRC64; MSVPTVLQKI LARKAEEVAE RRARVNLAEV ERLARSADAP RGFANALLER AKRKEPAVIA EIKKASPSKG VLREHFVPAE IARSYEAGGA ACLSVLTDVD FFQGADAYLK EARAACALPV IRKDFMIDPY QIVEARAIGA DCILLIVSAL DDVLMAELAA TAKSVGLDVL VEVHDGTELE RALKTLDTPL VGINNRNLHT FEVSLETTLD LLPEIPRDRL VVTESGILNR ADVELMEVSE VYAFLVGEAF MRADDPGLEL KRLFFQERGA VVLGADPD //