ID A0A2C5Y5H9_9HYPO Unreviewed; 759 AA.
AC A0A2C5Y5H9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CDD81_6759 {ECO:0000313|EMBL:PHH62690.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH62690.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH62690.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH62690.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH62690.1}.
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DR EMBL; NJET01000065; PHH62690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Y5H9; -.
DR STRING; 1399860.A0A2C5Y5H9; -.
DR OrthoDB; 294181at2759; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000226192; 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; 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; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 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 {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|PIRNR:PIRNR001382};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Isomerase {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:UP000226192};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|PIRNR:PIRNR001382}.
FT DOMAIN 29..217
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 247..509
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 596..753
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 759 AA; 82715 MW; 887BBD50A151B784 CRC64;
MASTAGLVDH SPHQPDASPP VPTASNLILI DNYDSFTWNI YQYLVLEGAT VHVFRNDQIT
LEELIEKKPT QLIISPGPGH PATDSGISRD VIRHFGGKVP IFGVCMGLQC MFDVYGGEVR
SAGEWLHGKT SPLTHDSKGV FADLEQRIPV TRYHSLAGTH VTLPECLEIS SWVANPDGSR
GIIQGIRHKV FAMEGVQFHP ESILTAHGRK MIKNFLLMQG GTWAENERLQ AERAASAPPK
PKGNNILQRI YASRKAAVAV ERQIPSQRME DLQAAYRLDA APPLVPFVNR LRQSPFDVAL
MAEIKRASPS KGIFALDINA PTQARKYALA GASVISVLTE PEWFKGSIQD LRAVRQVLDG
MPNRPAILRK DFIFDEYQIL EARLEGADTI LLIVKMLDQA LLQRLYDYSV SLGMEPLVEV
QNAQEMTIAV KLGAKVIGVN NRNLESFEVD LDTTGRLRSM VPEQTLICAL SGINTHDDVL
MNKKDGVNAV LVGEAIMRAP DASVFISELC SGSKPPIKEP SPPSLMVKIC GTRSVEAAQH
AVESGADFVG ICLVPSAKRC ISHDAALAIS KAIHSFTGSQ TSREQPAKLA ADTAIDFFAS
TDKRLGSRRP RLVGIFQNQP LSDVLDKQRQ YNLDMVQLHG DEPIEWARLI PVPVIRCFKP
GQVGIGKRGY HVLPLLDSGS GSGKMLDVSR VKAVLQQDPD LRVLLAGGLN PDNVASAVEA
LGELGHRVLG VDVSSGVEVD GKQDLDKISA FIKAAKGFR
//
