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Database: UniProt
Entry: G2X6F6_VERDV
LinkDB: G2X6F6_VERDV
Original site: G2X6F6_VERDV 
ID   G2X6F6_VERDV            Unreviewed;       773 AA.
AC   G2X6F6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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=VDAG_05738 {ECO:0000313|EMBL:EGY14574.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY14574.1};
RN   [1] {ECO:0000313|EMBL:EGY14574.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY14574.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA   Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL   Submitted (MAR-2008) 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}.
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DR   EMBL; DS572705; EGY14574.1; -; Genomic_DNA.
DR   RefSeq; XP_009653430.1; XM_009655135.1.
DR   AlphaFoldDB; G2X6F6; -.
DR   STRING; 498257.G2X6F6; -.
DR   MEROPS; C26.959; -.
DR   EnsemblFungi; EGY14574; EGY14574; VDAG_05738.
DR   GeneID; 20707201; -.
DR   KEGG; vda:VDAG_05738; -.
DR   eggNOG; KOG0026; Eukaryota.
DR   eggNOG; KOG4201; Eukaryota.
DR   eggNOG; KOG4202; Eukaryota.
DR   HOGENOM; CLU_007713_2_0_1; -.
DR   InParanoid; G2X6F6; -.
DR   OMA; FLHMQGG; -.
DR   OrthoDB; 294181at2759; -.
DR   UniPathway; UPA00035; UER00040.
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   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|PIRNR:PIRNR001382}.
FT   DOMAIN          28..216
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          258..520
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
FT   DOMAIN          608..764
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
FT   REGION          226..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   773 AA;  83380 MW;  4418220063508B00 CRC64;
     MPSLDIIDHS PHHPDPSPPI PTASNLILID NYDSFTWNVY QYLILEGANV TVYRNDKITL
     EELASKNPTQ LIISPGPGHP STDSGVSRDA IRHFAGKIPI FGVCMGQQCI FDVYGGEVSS
     AGEWLHGKTS PLTHDGKGVY AGLPQELPVT RYHSLAGTQV TLPSCLEVTS WVAKSDGSPG
     VIQGVRHREY TIEGVQFHPE SILTAEGRTM LKNFLLLQGG TWEENSRLQK ASASNGAASN
     GTPAQPAPPA AGKKNNILQQ IYDRRRKSVA AQKEIPSQRP ADLQATYDLN GAPPQIPFVA
     RLRQTPFDVA LMAEIKRASP SKGIFDLSIS APTQARKYAL AGASVISVLT EPDWFRGSIE
     DLRAVRQVLD GMPNRPAILR KEFIFEEYQI LEARLAGADT VLLIVKMLTV EELERLYKYS
     VSLGMEPLVE VQNTEEMTIA LNLGAKAIGV NNRNLESFEV DMGTTSRLRS MVPENTIICA
     LSGINTYDDV LLCKKDGVNA VLVGEAIMRA SDTTKFIRQL CSGSDAEPQK PAPEPLFAKI
     CGTRTPEAAE EAVRSGADFI GICLVTGAKR CISDDTALAI SQVVHSSSPA RFLPPVGSSA
     AGKVATDFFS SAKTRLSGSR TLLAGIFQNQ PLDEVLHKQK LFNLDIVQLH GDEPIEWASL
     IPVPVIRAFK PGQVGIGRRG YHTVPLLDSG AGSGKLLDFS SVTATLAQDP ELRIMLAGGL
     NPDNVVDAVR ALGKYASQVI GVDVSSGVEQ DGKQSLEKIR AFIKAAKSCH VVA
//
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