TRPG_CRYNH
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 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=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 EnsemblFungi; AFR97220; AFR97220; CNAG_04501.
DR GeneID; 23887910; -.
DR VEuPathDB; FungiDB:CNAG_04501; -.
DR HOGENOM; CLU_007713_2_0_1; -.
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; 3.20.20.70; -; 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_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
