TRPG_ASPNG
ID TRPG_ASPNG Reviewed; 770 AA.
AC P05328;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 141.
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 niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=401;
RX PubMed=2836085; DOI=10.1007/bf00365648;
RA Kos T., Kuijvenhoven A., Hessing H.G.M., Pouwels P.H.,
RA van den Hondel C.A.M.J.J.;
RT "Nucleotide sequence of the Aspergillus niger trpC gene: structural
RT relationship with analogous genes of other organisms.";
RL Curr. Genet. 13:137-144(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69 AND 392-433.
RX PubMed=2936650; DOI=10.1016/0378-1119(85)90317-8;
RA Kos A., Kuijvenhoven J., Wernars K., Bos C.J., van den Broek H.W.J.,
RA Pouwels P.H., van den Hondel C.A.M.J.J.;
RT "Isolation and characterization of the Aspergillus niger trpC gene.";
RL Gene 39:231-238(1985).
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; X07071; CAA30107.1; -; Genomic_DNA.
DR EMBL; M14403; AAA32710.1; -; Genomic_DNA.
DR EMBL; M14404; AAA32709.1; -; Genomic_DNA.
DR PIR; S00643; S00643.
DR AlphaFoldDB; P05328; -.
DR SMR; P05328; -.
DR STRING; 5061.CADANGAP00006800; -.
DR MEROPS; C26.959; -.
DR PRIDE; P05328; -.
DR VEuPathDB; FungiDB:An08g06080; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1129421; -.
DR VEuPathDB; FungiDB:ATCC64974_101700; -.
DR VEuPathDB; FungiDB:M747DRAFT_261847; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR eggNOG; KOG4202; Eukaryota.
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..770
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056855"
FT DOMAIN 25..225
FT /note="Glutamine amidotransferase type-1"
FT REGION 228..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..519
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 535..770
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT COMPBIAS 228..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 104
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 108
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 154..155
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
SQ SEQUENCE 770 AA; 82910 MW; 36D8DE5B23097012 CRC64;
MADSGLVDHS PHHPTKAAQL STASNVILID NYDSFTWNVY QYLVLEGATV NVFRNDQITL
EELIAKKPTQ LVISPGPGHP ETDAGISSAA IQYFSGKIPI FGVCMGQQCI ITCFGGKVDV
TGEILHGKTS PLKHDGKGAY EGLPGSLAVT RYHSLAGTHA TIPDCLEVSS SVQLADDSNK
DVIMGVRHKK LAVEGVQFHP ESILTEYGRI MFRNFLKLTA GTWEGNGKHF GEQSSTTKAT
VPSNPPPKTD KKLSILERIY DHRRAAVAVQ KTIPSQRPAD LQAAYDLNLA PPQIPFPARL
RQSPYPLSLM AEIKRASPSK GMIAENACAP AQARQYAKAG ASVISVLTEP EWFKGSIDDL
RAVRQSLEGM TNRPAILRKE FVFDEYQILE ARLAGADTVL LIVKMLSVEL LTRLYHYSRS
LGMEPLVEVN TPEEMKIAVD LGAEVIGVNN RDLTSFEVDL GTTSRLMDQV PSSTIVCALS
GISGPKDVEA YKKEGVKAIL VGEALMRAAD TATFIAELLG GSSQTVSSES RRSPLVKICG
TRSEEAARAA IEAGADLIGI IMVQGRTGCV PDDVALPISQ VVRSTPKPAS QALHTSQEPP
AATSVEYFDH SAKILRHPSR ALLVGVFQNQ PLDYILSQQQ KLGLDVVQLH GSEPLEWAKL
IPVPVIRKFG LDEPAIARRA YHSLPLLDSG VGGTGELLDQ SRVQNVLDKD CGLRVILAGG
LDPTNVAGIV QKLGESGRKV VGVDVSSGVE SDGAQDLNKI RAFVQAVRGL
