ID   TRPG_ASPAW              Reviewed;         768 AA.
AC   P18483;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   27-MAR-2024, entry version 131.
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   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 22342 / NRRL 3112;
RX   PubMed=2395660; DOI=10.1093/nar/18.16.4931;
RA   Adams R.R., Royer T.;
RT   "Complete genomic sequence encoding trpC from Aspergillus niger var.
RT   awamori.";
RL   Nucleic Acids Res. 18:4931-4931(1990).
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.
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DR   EMBL; X53576; CAA37640.1; -; Genomic_DNA.
DR   PIR; S11161; S11161.
DR   AlphaFoldDB; P18483; -.
DR   SMR; P18483; -.
DR   MEROPS; C26.959; -.
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; 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; 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..768
FT                   /note="Multifunctional tryptophan biosynthesis protein"
FT                   /id="PRO_0000056854"
FT   DOMAIN          25..223
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          253..517
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          533..768
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   768 AA;  82657 MW;  E3C0DB1AB10225CE CRC64;
     MADSGLVDHS PHHPTKAAQL NTASNVILID NYDSFTWNVY LVLEGATVNV FRNDQITLEE
     LIAKKPTQLV ISPGPGHPET DAGISSAAIQ YFSGKIPIFG VCMGQQCIIT CFGGKVDVTG
     EILHGKTSAL KHDGKGAYEG LPDSLALTRY HSLAGTHATI PDCLEVSSSV QLTDDSNKDV
     IMGVRHKKLA VEGVQFHPES ILTEYGRTMF RNFLKLTAGT WEGNGKHFDE QSNTTKATVS
     SNTAPKTDKK LSILERIYDH RRAAVAVQKT IPSQRPADLQ AAYDLNLAPP QVPFPARLRQ
     SPYPLSLMAE IKRASPSKGM IAENACAPAQ ARQYAKAGAS VISVLTEPEW FKGSIDDLRA
     VRQSLEGLTN RPAILRKEFV FDEYQILEAR LAGADTVLLI VKMLSVELLT RLYHYSRSLG
     MEPLVEVNTP EEMKIAVDLG AEVIGVNNRD LTSFEVDLGT TSRLMDQVPS STIVCALSGI
     SGPKDVEAYK KEGVKAILVG EALMRAADTA AFIAELLGGS SQNVSKESRS SPLVKICGTR
     SEEAARAAIE AGADLIGIIM VQGRTRCVPD DVALRISQVV KSIPKPAGQT PPTSRGTPAA
     ASVEYFDHSA RILRHPSRAL LVGVFQNQPL DYILSQQQKL GLDVVQLHGS EPLEWAKLIP
     VPVIRKFGLD EPAIARRAYH SLPLLDSGVG GTGELLDQSR VQNVLDKDSG LRVILAGGLD
     PTNVAGIVQK LGESGRKVVG VDVSSGVESD GAQDLGKIRA FVQAVRGL
//