ID A0A1B8CFS3_9PEZI Unreviewed; 762 AA.
AC A0A1B8CFS3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=VE00_03965 {ECO:0000313|EMBL:OBT45671.1};
OS Pseudogymnoascus sp. WSF 3629.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT45671.1, ECO:0000313|Proteomes:UP000091997};
RN [1] {ECO:0000313|EMBL:OBT45671.1, ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT45671.1,
RC ECO:0000313|Proteomes:UP000091997};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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}.
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DR EMBL; KV454591; OBT45671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8CFS3; -.
DR STRING; 1622147.A0A1B8CFS3; -.
DR OrthoDB; 294181at2759; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000091997; 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:UP000091997};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|PIRNR:PIRNR001382}.
FT DOMAIN 28..217
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 251..513
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 569..756
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 762 AA; 82218 MW; 3EC59FF65FA275EA CRC64;
MPSLELIDHS PHGHAAVAPL ENASNLIMID NYDSFTWNIY QYLVLEGATV TVYRNDKITV
EELAAKKPTQ LVISPGPGHP SSDSGVSRDA IKHFAGKIPV LGVCMGQQCI FSVFGGEVSY
AGEILHGKTS PLRHDSNGMY AGLPQDLPVT RYHSLAGTHP TLPEALEVTS WIASPENNDG
KGVIMGVRHK EYVVEGVQFH PESILTEEGR VMLKNFLNMR GGTWAENERL QKEAASKATP
AAASSQKENI LDKIFAHRKA AVAAQKQLPS QRPSDLQASY DMNLSPPNIS FVDRLRLSPY
PLSLMAEVKR ASPSKGIISI STCAPAQAME YALAGASVIS VLTEPEWFKG SIDDLRYVRQ
ALEGMPNRPA ILRKEFIFEE YQILEARLAG ADTVLLIVKM LDEATLQRLY SYSLTLGMEP
LVEVNTADEM KVAVDLGAKV IGVNNRNLAS FEVDLETTSR LMSQVPETTI VCALSGISGP
QDVESYKKNG VGAVLVGEAL MRASDKPKFI AELLGGSLDA PAKAPEQPLL VKICGTRSAK
AAATAVAAGA DFVGMILVPG RKRTVSEEEG LAISEVVHKA TPRAVKTNSQ IKATAGSDFF
AAAASTLTSA RPLLVGVFQN QSLEEVLRLQ KLFSLDIVQL HGDEPLEWSK LIPVPVVKSF
RPEQVNIGSR GYHTVPLLDS ATGGSGEKLD MSKVRETLQK DKRLRVMLAG GLNADNVVEA
LREVGELSSR IIGVDVSSGV EEGGVQDLDK IISFIKSAKS VR
//
