TRPG_PENCH
ID TRPG_PENCH Reviewed; 752 AA.
AC P24773;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3103104; DOI=10.1093/nar/15.4.1874;
RA Penalva M.A., Sanchez F.;
RT "The complete nucleotide sequence of the trpC gene from Penicillium
RT chrysogenum.";
RL Nucleic Acids Res. 15:1874-1874(1987).
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; X05033; CAA28707.1; -; Genomic_DNA.
DR PIR; S30084; S30084.
DR AlphaFoldDB; P24773; -.
DR SMR; P24773; -.
DR MEROPS; C26.959; -.
DR PhylomeDB; P24773; -.
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..752
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056862"
FT DOMAIN 23..223
FT /note="Glutamine amidotransferase type-1"
FT REGION 239..503
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 519..752
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 752 AA; 81035 MW; D6256C3818E22FDB CRC64;
MADLVDHSPH HATKAAKLAS ASNVILIDNY DSFTWNIYQY LVLEGATVTV YRNDEVTVED
LVAKKPTQLV ISPGPGHPDT DAGISNAVIK HFSGKVPIFG VCMGQQCMIT SFGGKVDVTG
EILHGKTSEL KHDSKGVYQG LPTSLEVTRY HSLAGTHSTI PDCLEVTSRV ELGDASGKNI
IMGVRHKEFA VEGVQFHPES ILTQYGRKMF RNFLELTAGT WDNKQGAAVA APADKKLSIL
DKIYAHRKNA VDEQKKIPAL RPEALQAAYD LNIAPPQLSF PDRLRQSDYP LSLMAEIKRA
SPSKGIISAN VCAPAQAREY AKAGASVISV LTEPEWFKGT IDDLRAVRQS LEGLPNRPAV
LRKEFVFEEY QILEARLAGA DTVLLIVKML DIELLTRLYH YSRSLGMEPL VEVNTPEEMK
IAVDLGSEVI GVNNRDLTSF EVDLGTTSRL MDQVPESTIV CALSGISGPQ DVEAYKKEGV
KAILVGEALM RAPDTSAFVA QLLGGSNQNF AGASPSSPLV KICGTRTEEG ALAAIQAGAD
LIGIIMVQGR SRLVPDDVAL GISRVVKSTP RPADTLQQPS SATSLEWFDH STNILRHPSR
ALLVGVFMNQ PLSYVVSQQQ KLGLDVVQLH GSEPLEWSSL IPVPVIRKFA PGDIGIARRA
YHTLPLLDSG AGGSGELLEE SGVKKVLDSD EGLRVILAGG LNPDNVAGTV KKLGQSGQKV
VGLDVSSGVE TNGAQDLEKI RAFVKSAKSI RQ
