ID TRPG_PENCH Reviewed; 752 AA. AC P24773; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 13-SEP-2023, entry version 129. DE RecName: Full=Multifunctional tryptophan biosynthesis protein; DE Includes: DE RecName: Full=Anthranilate synthase component 2; DE Short=AS; DE EC=4.1.3.27; DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component; DE Includes: DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; DE Includes: DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpC; OS Penicillium chrysogenum (Penicillium notatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium; OC Penicillium chrysogenum species complex. OX NCBI_TaxID=5076; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3103104; DOI=10.1093/nar/15.4.1874; RA Penalva M.A., Sanchez F.; RT "The complete nucleotide sequence of the trpC gene from Penicillium RT chrysogenum."; RL Nucleic Acids Res. 15:1874-1874(1987). CC -!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase CC (GATase) domain of anthranilate synthase, indole-glycerolphosphate CC synthase, and phosphoribosylanthranilate isomerase activities. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2- CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; CC EC=5.3.1.24; 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 -!- CATALYTIC ACTIVITY: CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58359; EC=4.1.3.27; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. 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; X05033; CAA28707.1; -; Genomic_DNA. DR PIR; S30084; S30084. DR AlphaFoldDB; P24773; -. DR SMR; P24773; -. DR MEROPS; C26.959; -. DR PhylomeDB; P24773; -. DR UniPathway; UPA00035; UER00040. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1. DR CDD; cd00331; IGPS; 1. DR CDD; cd00405; PRAI; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 2. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016302; Anthranilate_synth_II. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR001240; PRAI_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR006221; TrpG/PapA_dom. DR NCBIfam; TIGR00566; trpG_papA; 1. DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1. DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00697; PRAI; 1. DR PIRSF; PIRSF001382; TrpG-trpC-trpF; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase; KW Glutamine amidotransferase; Isomerase; Lyase; Multifunctional enzyme; KW Tryptophan biosynthesis. FT CHAIN 1..752 FT /note="Multifunctional tryptophan biosynthesis protein" FT /id="PRO_0000056862" FT DOMAIN 23..223 FT /note="Glutamine amidotransferase type-1" FT REGION 239..503 FT /note="Indole-3-glycerol phosphate synthase" FT REGION 519..752 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT ACT_SITE 102 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000250|UniProtKB:P00900" FT ACT_SITE 197 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT ACT_SITE 199 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT BINDING 74..76 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 106 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 152..153 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" SQ SEQUENCE 752 AA; 81035 MW; D6256C3818E22FDB CRC64; MADLVDHSPH HATKAAKLAS ASNVILIDNY DSFTWNIYQY LVLEGATVTV YRNDEVTVED LVAKKPTQLV ISPGPGHPDT DAGISNAVIK HFSGKVPIFG VCMGQQCMIT SFGGKVDVTG EILHGKTSEL KHDSKGVYQG LPTSLEVTRY HSLAGTHSTI PDCLEVTSRV ELGDASGKNI IMGVRHKEFA VEGVQFHPES ILTQYGRKMF RNFLELTAGT WDNKQGAAVA APADKKLSIL DKIYAHRKNA VDEQKKIPAL RPEALQAAYD LNIAPPQLSF PDRLRQSDYP LSLMAEIKRA SPSKGIISAN VCAPAQAREY AKAGASVISV LTEPEWFKGT IDDLRAVRQS LEGLPNRPAV LRKEFVFEEY QILEARLAGA DTVLLIVKML DIELLTRLYH YSRSLGMEPL VEVNTPEEMK IAVDLGSEVI GVNNRDLTSF EVDLGTTSRL MDQVPESTIV CALSGISGPQ DVEAYKKEGV KAILVGEALM RAPDTSAFVA QLLGGSNQNF AGASPSSPLV KICGTRTEEG ALAAIQAGAD LIGIIMVQGR SRLVPDDVAL GISRVVKSTP RPADTLQQPS SATSLEWFDH STNILRHPSR ALLVGVFMNQ PLSYVVSQQQ KLGLDVVQLH GSEPLEWSSL IPVPVIRKFA PGDIGIARRA YHTLPLLDSG AGGSGELLEE SGVKKVLDSD EGLRVILAGG LNPDNVAGTV KKLGQSGQKV VGLDVSSGVE TNGAQDLEKI RAFVKSAKSI RQ //