ID TRPG_PHYBL Reviewed; 765 AA. AC P20409; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 04-NOV-2026, entry version 142. 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=trp1; OS Phycomyces blakesleeanus. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces. OX NCBI_TaxID=4837; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2823101; DOI=10.1128/mcb.7.8.2664-2670.1987; RA Revuelta J.L., Jayaram M.; RT "Phycomyces blakesleeanus TRP1 gene: organization and functional RT complementation in Escherichia coli and Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 7:2664-2670(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3215529; DOI=10.1016/0378-1119(88)90080-7; RA Choi H.T., Revuelta J.L., Sadhu C., Jayaram M.; RT "Structural organization of the TRP1 gene of Phycomyces blakesleeanus: RT implications for evolutionary gene fusion in fungi."; RL Gene 71:85-95(1988). 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 + pyruvate + L- CC glutamate + H(+); Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, CC ChEBI:CHEBI:29985, 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; M17240; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M17241; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M23177; AAA33633.1; -; Genomic_DNA. DR PIR; JT0383; JT0383. DR AlphaFoldDB; P20409; -. DR SMR; P20409; -. DR MEROPS; C26.959; -. DR VEuPathDB; FungiDB:PHYBLDRAFT_124173; -. DR OMA; AAYDLNC; -. DR UniPathway; UPA00035; UER00040. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0000162; P:L-tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1. DR CDD; cd00331; IGPS; 1. DR CDD; cd00405; PRAI; 1. DR FunFam; 3.20.20.70:FF:000136; Multifunctional tryptophan biosynthesis protein; 1. DR FunFam; 3.40.50.880:FF:000031; Multifunctional tryptophan biosynthesis protein; 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; IPR050472; Anth_synth/Amidotransfase. 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; 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..765 FT /note="Multifunctional tryptophan biosynthesis protein" FT /id="PRO_0000056864" FT DOMAIN 2..196 FT /note="Glutamine amidotransferase type-1" FT REGION 231..494 FT /note="Indole-3-glycerol phosphate synthase" FT REGION 512..765 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT ACT_SITE 81 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000250|UniProtKB:P00900" FT ACT_SITE 170 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT ACT_SITE 172 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT BINDING 53..55 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 85 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 131..132 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT CONFLICT 606 FT /note="I -> T (in Ref. 2; AAA33633)" FT /evidence="ECO:0000305" FT CONFLICT 617 FT /note="G -> A (in Ref. 2; AAA33633)" FT /evidence="ECO:0000305" SQ SEQUENCE 765 AA; 83423 MW; BDE6D904C065F58C CRC64; MATLLIDNYD SFTYNVYQYL CSQGADVVVY RNDKITVDEI VKLNPVNIVI SPGPGHPSHD AGVSRDVISY FAGKLPILGI CMGEQCIFEV FGGTVSYAGD ILHGKTSTIK HDNRGLFKNV PQDNQVTRYH SLAGMPSTLP EVLEVTATTD DGVIMGVRHK KYTVEGVQFH PESILCEHGH TMISNFLSLR GGNWDENPAA GVLAQKVPAA ATEKAAQEAS PAISTPPTCS TILSRIYAQR VKDVQAAKEV PGQSQADLQK LLNLHIAPPL RDVVNRLKES SPALMAEVKR ASPSKGNIDI TVNAAEQALQ YALAGASVIS VLTEPKWFRG SLNDLRQVRE ACPLLPNRPC ILRKTFLLDT YQILEARLYG ADTVLLIVAM MSDEDLRELY QYSVSLGMEP LVEVNNAEEM ARANAVGAKL IGVNNRGLHS FDVDMETTSR LAEMVPEGTI LCALSGISTR ADVETYVSQG VHGLLVGEAL MRAWNLKEFV AELLGYKKKD PVPHTPVSRQ VQVKICGISS VEAAVEAATA GADLVGLIFA EKSKRQVTVA KAREIVDALH KLPTRSSQLP VKSQKSIDWF DVQTEMVEQR VPWRPLVVGV FVNQSIEYMS QVAVEAGLDL IQLHGTESAE IARFLPVPVI KAFHMDASSF HAGQIPYVTQ PGNNQLLLLD AKVPSLPMDR QGGLGQKFDW TIAQDIVNVK RPGCSKEQTF PVILAGGLDP SNISEAIQQV RPWAVDVSSG VETDGKKDLK KIRAFVEKAK SINLQ //