TRPG_ASPAW
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 03-AUG-2022, entry version 127.
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; 3.20.20.70; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
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 Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
DR SUPFAM; SSF51366; SSF51366; 2.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
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
