TRPG_PHYBL
ID TRPG_PHYBL Reviewed; 765 AA.
AC P20409;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Phycomyces blakesleeanus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=4837;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2823101; DOI=10.1128/mcb.7.8.2664-2670.1987;
RA Revuelta J.L., Jayaram M.;
RT "Phycomyces blakesleeanus TRP1 gene: organization and functional
RT complementation in Escherichia coli and Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:2664-2670(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3215529; DOI=10.1016/0378-1119(88)90080-7;
RA Choi H.T., Revuelta J.L., Sadhu C., Jayaram M.;
RT "Structural organization of the TRP1 gene of Phycomyces blakesleeanus:
RT implications for evolutionary gene fusion in fungi.";
RL Gene 71:85-95(1988).
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; M17240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M17241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M23177; AAA33633.1; -; Genomic_DNA.
DR PIR; JT0383; JT0383.
DR AlphaFoldDB; P20409; -.
DR SMR; P20409; -.
DR MEROPS; C26.959; -.
DR VEuPathDB; FungiDB:PHYBL_124173; -.
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..765
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056864"
FT DOMAIN 2..196
FT /note="Glutamine amidotransferase type-1"
FT REGION 231..494
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 512..765
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT ACT_SITE 81
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT ACT_SITE 170
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 172
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 53..55
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 85
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 131..132
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 606
FT /note="I -> T (in Ref. 2; AAA33633)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="G -> A (in Ref. 2; AAA33633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 83423 MW; BDE6D904C065F58C CRC64;
MATLLIDNYD SFTYNVYQYL CSQGADVVVY RNDKITVDEI VKLNPVNIVI SPGPGHPSHD
AGVSRDVISY FAGKLPILGI CMGEQCIFEV FGGTVSYAGD ILHGKTSTIK HDNRGLFKNV
PQDNQVTRYH SLAGMPSTLP EVLEVTATTD DGVIMGVRHK KYTVEGVQFH PESILCEHGH
TMISNFLSLR GGNWDENPAA GVLAQKVPAA ATEKAAQEAS PAISTPPTCS TILSRIYAQR
VKDVQAAKEV PGQSQADLQK LLNLHIAPPL RDVVNRLKES SPALMAEVKR ASPSKGNIDI
TVNAAEQALQ YALAGASVIS VLTEPKWFRG SLNDLRQVRE ACPLLPNRPC ILRKTFLLDT
YQILEARLYG ADTVLLIVAM MSDEDLRELY QYSVSLGMEP LVEVNNAEEM ARANAVGAKL
IGVNNRGLHS FDVDMETTSR LAEMVPEGTI LCALSGISTR ADVETYVSQG VHGLLVGEAL
MRAWNLKEFV AELLGYKKKD PVPHTPVSRQ VQVKICGISS VEAAVEAATA GADLVGLIFA
EKSKRQVTVA KAREIVDALH KLPTRSSQLP VKSQKSIDWF DVQTEMVEQR VPWRPLVVGV
FVNQSIEYMS QVAVEAGLDL IQLHGTESAE IARFLPVPVI KAFHMDASSF HAGQIPYVTQ
PGNNQLLLLD AKVPSLPMDR QGGLGQKFDW TIAQDIVNVK RPGCSKEQTF PVILAGGLDP
SNISEAIQQV RPWAVDVSSG VETDGKKDLK KIRAFVEKAK SINLQ
