ID TRPG_CRYNJ Reviewed; 752 AA. AC P0CN86; Q55NN6; Q5KC22; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 68. 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; OrderedLocusNames=CNI00560; OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC OS MYA-565) (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=214684; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21 / ATCC MYA-565; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). 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; AE017349; AAW45488.1; -; Genomic_DNA. DR RefSeq; XP_572795.1; XM_572795.1. DR AlphaFoldDB; P0CN86; -. DR SMR; P0CN86; -. DR STRING; 214684.P0CN86; -. DR MEROPS; C26.959; -. DR PaxDb; 214684-P0CN86; -. DR EnsemblFungi; AAW45488; AAW45488; CNI00560. DR GeneID; 3259660; -. DR KEGG; cne:CNI00560; -. DR VEuPathDB; FungiDB:CNI00560; -. DR eggNOG; KOG0026; Eukaryota. DR eggNOG; KOG4201; Eukaryota. DR eggNOG; KOG4202; Eukaryota. DR HOGENOM; CLU_007713_2_0_1; -. DR InParanoid; P0CN86; -. DR OMA; EPIEWAN; -. DR OrthoDB; 294181at2759; -. DR UniPathway; UPA00035; UER00040. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000002149; Chromosome 9. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IEA:EnsemblFungi. 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; IBA:GO_Central. 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; IPR045186; Indole-3-glycerol_P_synth. 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; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 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 Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..752 FT /note="Multifunctional tryptophan biosynthesis protein" FT /id="PRO_0000056857" FT DOMAIN 3..202 FT /note="Glutamine amidotransferase type-1" FT REGION 231..495 FT /note="Indole-3-glycerol phosphate synthase" FT REGION 509..752 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT ACT_SITE 86 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000250|UniProtKB:P00900" FT ACT_SITE 176 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT ACT_SITE 178 FT /note="For GATase activity" FT /evidence="ECO:0000250" FT BINDING 58..60 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 136..137 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" SQ SEQUENCE 752 AA; 80473 MW; BE85651BED85BBE5 CRC64; MGFTLLIDNY DSFTWNIYAD LASVGGNPYV VRNDKITLKE IEGMFSDGEL ERIVISPGPG HPRTDSGVSR DVIAWGMGKL PILGVCMGLE CIVDLLGGEI AYAGEIKHGK TSLVQHDSIG VFHNLPQFLS STRYHSLSAQ IQSLPSVLQV TSTTKESGVI MGVRHRTYTV EAVQYHPESC MSEGGRGLMA NFIQMKGGKW GGENAWCGVP AEGEEEQPKA KTNGAPSLPT ILNRIHAQRL LDVEQAEKVP ATSPANVSTS LSLYASPPLI NFRDRMVSTP HTAVMAEIKR ASPSKGDIAP TASAPEQALK YALAGASVIS VLTEPTWFKG SLLDMLAVRN AVDSLPNRPA ILRKDFVLSK YMIDEARLYG ADTVLLIVAM LEPQQLKELY DYSVSLGMEP LVEVNNPTEL SLALEIGSKV IGVNNRNLHD FNVDMSTTSR VNAALNGRDV VLCALSGISS HEDVEKYVKE GVKGVLVGEA LMRASDTKAF LRSLIGLPPL EVVPKSRPLV KICGIRSTDD AKLAISAGAD LLGVILVPGT KRCISTSTAR EISALVQSAR SQSSSKPLEP SLSSPWFTTQ SDLLSSRRKP LLVGVFQNQS LSDILSAVEE IGLDLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE FRRPGLNQAI LLDAGGVSGG GGEGKAFPWE HAKRLIQSGE VGSEGHMPLP VILAGGLTPE NVGQAIEQAG EGVWCVDVSS GVEGEGGKVK EKVEAFVKAV RG //