TRPG_COCHE
ID TRPG_COCHE Reviewed; 768 AA.
AC Q92411;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris
OS maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5016;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 48330 / C3;
RA Mullin P.G., Turgeon B.G., Yoder O.C.;
RT "Complementation of Cochliobolus heterostrophus trp-mutants produced by
RT gene replacement.";
RL Fungal Genet. Newsl. 40:51-53(1993).
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; X70035; CAA49629.1; -; Genomic_DNA.
DR AlphaFoldDB; Q92411; -.
DR SMR; Q92411; -.
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_0000056856"
FT DOMAIN 25..225
FT /note="Glutamine amidotransferase type-1"
FT REGION 256..520
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 535..768
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT ACT_SITE 103
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT ACT_SITE 199
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 76..78
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 153..154
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
SQ SEQUENCE 768 AA; 83655 MW; B2F215AA304B8B00 CRC64;
MPSSTLIDHS PRNPNPSPPR ITASNVILID NYDSFTWNVY QYLVFEGAFV TVYRNDEITL
DELIAKKPTQ LVISQVPDTR KEDVALAIEP LRTSVAKSPF SACAWESCIF YSYGGTVDVT
GQILHGKTCP LKHDGKGVFA GVPQDVPVTR YHSLAGTHGT LPDCLEISAT IPANADAEIK
EVIMGVRHKE YVIEGVQFHP ESILTEHGRL MMRNFLKMQG GTWAENERLQ KEAHAQAIGA
AFSESAMVQR TDSRTHLQKI YDHRRAAVAE QKKIPSNRPV DLQAAYDSNL APPQINFPER
LRQSPFKLSL MSEIKRASPS KGIISLSTCA PAQARLYAKA GARPISVLTE PEWFKGSIED
LRAVRQSIEG MANRPALLRK EFIFDEYQIL EGRLAGADTV LVIVKMLETE LLERLLGLSD
SVGMEPLVEV QNTDEMKIAV KLGAQVIGVN NRNLVNFEVD IGTTNRLIQM VPKETILCAL
SGIAGPKDVE AYIKDGVGAV LVGEALMRAS DMSQFISELL GGPYKEVRAS SSSPIVKISG
TRSEAAVAAV EAGADLIGII LAPGLKRTVT AETALSISEA VHKTKKPNVS KSGLLADSKT
ASDFFDHGAS RLLETISRAL LVGVFRNQSL EYVLEQQRLL NLDVVQLHGQ EPIEWAKLVP
VPVLKAFNPQ DHGIGTRGYH ALPLLDAGSG GSGKQLGLSD VKAAFTKDDG IKIILGRGLE
PDNVQTTLAG LDEYRDRVYA VDVSSGVEED GQQSLDKIRS FVKAAKSL
