TRPG_PHACH
ID TRPG_PHACH Reviewed; 788 AA.
AC P25170;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750;
RX PubMed=2041479; DOI=10.1111/j.1365-2958.1991.tb02130.x;
RA Schrank A., Tempelaars C., Sims P.F.G., Oliver S.G., Broda P.;
RT "The trpC gene of Phanerochaete chrysosporium is unique in containing an
RT intron but nevertheless maintains the order of functional domains seen in
RT other fungi.";
RL Mol. Microbiol. 5:467-476(1991).
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; X56047; CAA39518.1; -; Genomic_DNA.
DR PIR; S15239; S15239.
DR AlphaFoldDB; P25170; -.
DR SMR; P25170; -.
DR VEuPathDB; FungiDB:AGR57_4754; -.
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: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; 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_00134_B; IGPS_B; 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..788
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056863"
FT DOMAIN 12..207
FT /note="Glutamine amidotransferase type-1"
FT REGION 238..503
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 520..788
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT ACT_SITE 91
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT ACT_SITE 181
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 63..65
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 141..142
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
SQ SEQUENCE 788 AA; 85345 MW; 20108D088803D787 CRC64;
MSLPPHLCVP IDILMIDNFD SFTWNLYQSL CLLGADVTVI RNDAIPRSAI PQLRIKRLIV
SPGPGHPQTD SGISREAIKY FAGKVPIMGV CMGLECVVDV FGGQIAYAGE IMHGKVSGIR
HDARGCFKDL PQGIQSTRYH SLSAGVKTLP DELAVTAVTE HERVIMGIRH RKYTVEAVQY
HPESILSESG DDLLRHFMKL KGGTWEENPE FRVLDPSLPA FEIGSQPAAS TSAKIPTILE
KICAQRQKDV DQAKATPGTT PEDLKTLLSM KLSPPQISFP DRLKAAEVKP ALMAEVKRAS
PSKGPIAMNG NAAQQALTYA LAGASVISVL TEPTWFKGSL LDMRLARQAI DNLPHRPAIL
RKDFIIDEYQ IDEARLHGAD TVLLIVATLT EKRLEELYAY SQSLGMEPLV EVNNAKEMEI
ALKLGAKVIG VNNRNLHDFN VDMGTTSRLA EMVRERDVIL CALSGIKDAQ DVNTYVEQGV
GAVLVGESLM RAPDTRAFIR QLLSIPESEA KGKGKETTPL SRSCGIRTEE EALAAAEAGA
DMLGLMFVPK SKRYVSLEKA QQIAAAIHSR RLSKPVLTSG KTLENEPWFT AQQPPSRSFV
WRFAARPLLV GVFQNQPLSV YLTPCVPQLD LVQLHGSEPA ELAKHYPVPV IRVFHVSADG
RGLADLARPG LHQFALLDAV LPGSASALSG GTGTTVDWAL ARDAVRSGEV RVARSAQGDG
PVLSLNSSEA LYPMPVILAG GPQPENVSEA VDTVAPWAVD VSGGVELEDG SGKDLEKVRA
FVKAAKKL
