ID A0A1J8QA47_9AGAM Unreviewed; 858 AA.
AC A0A1J8QA47;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Multifunctional tryptophan biosynthesis protein {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=Anthranilate synthase component 2 {ECO:0000256|PIRNR:PIRNR001382};
DE Short=AS {ECO:0000256|PIRNR:PIRNR001382};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001382};
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|PIRNR:PIRNR001382};
DE Short=IGPS {ECO:0000256|PIRNR:PIRNR001382};
DE EC=4.1.1.48 {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|PIRNR:PIRNR001382};
DE Short=PRAI {ECO:0000256|PIRNR:PIRNR001382};
DE EC=5.3.1.24 {ECO:0000256|PIRNR:PIRNR001382};
GN ORFNames=AZE42_09360 {ECO:0000313|EMBL:OJA16851.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA16851.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA16851.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA16851.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase
CC (GATase) domain of anthranilate synthase, indole-glycerolphosphate
CC synthase, and phosphoribosylanthranilate isomerase activities.
CC {ECO:0000256|ARBA:ARBA00003272, ECO:0000256|PIRNR:PIRNR001382}.
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 Evidence={ECO:0000256|ARBA:ARBA00001633,
CC ECO:0000256|PIRNR:PIRNR001382};
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; Evidence={ECO:0000256|ARBA:ARBA00001164,
CC ECO:0000256|PIRNR:PIRNR001382};
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 Evidence={ECO:0000256|ARBA:ARBA00000329,
CC ECO:0000256|PIRNR:PIRNR001382};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJA16851.1}.
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DR EMBL; LVVM01002327; OJA16851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QA47; -.
DR STRING; 180088.A0A1J8QA47; -.
DR OrthoDB; 294181at2759; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
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; 2.
DR PIRSF; PIRSF001382; TrpG-trpC-trpF; 2.
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 {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001382};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|PIRNR:PIRNR001382};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW ECO:0000256|PIRNR:PIRNR001382};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR001382};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001382};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|PIRNR:PIRNR001382}.
FT DOMAIN 18..202
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 250..517
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 627..677
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT DOMAIN 795..851
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 858 AA; 92251 MW; 13A162B187BBCA93 CRC64;
MSTPPSLPAA LSGHIDTLMI DNFDSFTWNL YQSLSLLGTQ VIVVRNDALT VDQLPLLHIN
RLIISPGPGH PKNDSGVSRD AIKYFAGKIP ILGVCMGLEC IVDVYGGEIG FAGEIKHGKL
SPITHDGRSV FLSLSQSILS TRYHSLSASL LSLPSCLMVT SATSDSGVIM GVRHRTYVVE
AVQYHPESIL SQEGEGLLRN FLSLRGGTWE ENPHAKVYDP EMPPFPYEAL SAKSKSVITD
AAKSSAPSIL TKIAKTRTSD VESLSNTPGL TLPALNAHLS LHLAPPPISL SQRLLQVRNG
MALLAEIKRA SPSAGPIALH TSAPHTALSY ALAGASAISV ITEPTYFHGH LEDMRAVRLA
IEGLDRRPAV LRKDFVLSEY QVVEARVAGA DSVLLIVAML GKDRTRELLE YSMSLGMEPL
VEVNSPSELH IALDVGAKII GVNNRNLHSF NVDMSTTSSV AEVLEQKGKT GEVILCALSG
IKGPADVRAY REQQVKAVLV GESLMRAEDK GKFVRHLLDL DDPLPPSSPE NPNTIFPTPL
VKICGILTAS EALRTANAGA DFLGLMFVPT SKRIVSVPLA REISLAVRNA FPLPESDDEE
DEDENLKLPL PWFTSHTRAS YLPSPTRKTR PLLVGVFQNQ PLRYIQRIVH DVGLDMVQLH
GSEPIEWARS IGVPVIRVGG VPPPSTPTPA PEEKAQIVDG ENKAEETQIA PLPTPDPLMA
LTIPGYHHFI LLDTTASAQS SSPGGGTGKI LDWTRATRLV SKGEVPVISP DVSVGASLVP
LIVNGDELPT SAFPLPLILA GGLNPSNVRE AVEVVRPWAV DVSGGVERDE IDDELVKQDG
RKDAEKVLAF VRAAKGMN
//
