ID   TRPG_CRYNH              Reviewed;         752 AA.
AC   P27710; J9VZN1;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   13-SEP-2023, entry version 130.
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; ORFNames=CNAG_04501;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-752.
RX   PubMed=1452032; DOI=10.1016/0378-1119(92)90053-r;
RA   Perfect J.R., Rude T.H., Penning L.M., Johnston S.A.;
RT   "Cloning the Cryptococcus neoformans TRP1 gene by complementation in
RT   Saccharomyces cerevisiae.";
RL   Gene 122:213-217(1992).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA51445.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAA51445.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP003828; AFR97220.1; -; Genomic_DNA.
DR   EMBL; M74901; AAA51445.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JN0451; JN0451.
DR   RefSeq; XP_012051839.1; XM_012196449.1.
DR   AlphaFoldDB; P27710; -.
DR   SMR; P27710; -.
DR   GeneID; 23887910; -.
DR   KEGG; cng:CNAG_04501; -.
DR   VEuPathDB; FungiDB:CNAG_04501; -.
DR   HOGENOM; CLU_007713_2_0_1; -.
DR   OrthoDB; 294181at2759; -.
DR   UniPathway; UPA00035; UER00040.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000010091; Chromosome 9.
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; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
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; IPR045186; Indole-3-glycerol_P_synth.
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   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
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_0000056858"
FT   DOMAIN          3..202
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          231..495
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          509..752
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT   ACT_SITE        86
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   ACT_SITE        176
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..60
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         136..137
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   CONFLICT        295..309
FT                   /note="KGDIAPTASAPQQAL -> FQGRNAPTLLLLRST (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="P -> S (in Ref. 2; AAA51445)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   752 AA;  80194 MW;  FE31FEF7BFC5FC91 CRC64;
     MGFTLLIDNY DSFTWNIYAD LASVGGNPFV VRNDKITLKE IEGMFADGEL ERIVISPGPG
     HPRTDSGVSR DVIAWGMGKL PILGVCMGLE CIVDLLGGEI AYAGEIKHGK TSLVQHDSIG
     VFHNLPQFLS STRYHSLSAQ IQSLPSVLQV TSTTKESGVI MGVRHRTFTV EAVQYHPESC
     MSEGGRGLMA NFIQMKGGKW GGENAWCGVP AEGEGEQPKA KTNGAPSLPT ILNKIHAQRL
     LDVEQAEKIP ATTPANVSTS LSLYTSPPLI NFRGRMVSTP HTAVMAEIKR ASPSKGDIAP
     TASAPQQALK YALAGASVIS VLTEPTWFKG SLLDMLAVRN AVDSLPNRPA ILRKDFVLSK
     YMIDEARLYG ADTVLLIVAM LEPQQLKELY DYSVSLGMEP LVEVNNPTEL SLALEIGSKV
     IGVNNRNLHD FNVDMSTTSR VNAALNGRDV VLCALSGISS HEDVEKYVKE GVKGVLVGEA
     LMRASDTKAF LRSLIGLPPL EVVPKPRPLV KICGIRSTND AKLAINAGAD LLGVILVPGT
     KRCISTSTAR EISALVQSAR SQSSSKPLEP SLSSPWFTSQ SALLSSRRKP LLVGVFQNQS
     LSDILSAVDE IGLDLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE IRRPGLNQAI
     LLDAGGASGG GGEGKAFPWE HAKRLIQSGE VGSEGHVPLP VILAGGLTPE NVGQAIEQAG
     EGVWCVDVSS GVEGEGGKVK EKVEAFVKAV RG
//