ID   A0A319DUR0_ASPSB        Unreviewed;       698 AA.
AC   A0A319DUR0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0000313|EMBL:PYI01416.1};
GN   ORFNames=BO78DRAFT_16933 {ECO:0000313|EMBL:PYI01416.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI01416.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI01416.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI01416.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004721}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase
CC       family. {ECO:0000256|ARBA:ARBA00038363}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase
CC       family. {ECO:0000256|ARBA:ARBA00038372}.
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DR   EMBL; KZ826416; PYI01416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DUR0; -.
DR   STRING; 1448318.A0A319DUR0; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046165; P:alcohol biosynthetic process; IEA:UniProt.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 2.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR12001:SF72; THIJ_PFPI FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G01210)-RELATED; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   Pfam; PF19086; Terpene_syn_C_2; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 2.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          347..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   698 AA;  78930 MW;  0E812A3D30E682E2 CRC64;
     MGRVFDTMAP TMELPMDTSY PVPRASPGIQ GFCEAYPLRR HNFEDRANGG SLQCRADWET
     YIGPTERWGC CNPWQGHFSA VVLPFCRPDR IAVISYIFEY AFLYDNVVES VAKSTLNINA
     DSIGLDEAEY RTVRSITGTK QIQSKMLLEL LSIDPQCGEV VLDAWKTMID TTAKQDKTRT
     FNSLQEYVDY RIIDTGAPFV DTLMRFGMGI LLTPEEGLIA PIVKPCYAAL GLANDYFSFD
     VEWEEFQKEG SDKKAMTNAV WLFKQWHHVD QDEAKRLVQQ VTNNYEKEYR QRVHECVSGE
     GKENARLQEY LVALGYQIPG NVAWSLHCPR YHPWLCEKAG AILQASSGEI PNPSTRQSIS
     GESLSSQSSL WSGASDNSPR SSISSAPSVD VTGKPSDRAD LGSEHVMGPA EYIGSLPSKG
     VREAFIDALN VWLILPDGQV NVLKSIARTL HNASLMLDDI EDSSPLRRGQ PATHMIFGQG
     PTINSANFLL IQAMDQVRQL EDSCCLDIFI EEMRNLFIGQ SHDLYWTRQG ECPTEDEYME
     MIRQKTGGLF RLLARLMMQK APAQKNRMTL DPLINLLGEY FQIRDDYKNL TEEYTGQKGF
     CEDLGEGKFS FPLIYALKSR PDDLELREIL QRARESGGLD VPSKQCVLDH FNQSGSMEYT
     QRTLRGLMEE LRDRISQVEK EAGSSNWVLR LLVHRLEV
//