ID S8ALE0_PENO1 Unreviewed; 448 AA.
AC S8ALE0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=geranylgeranyl diphosphate synthase {ECO:0000256|ARBA:ARBA00012382};
DE EC=2.5.1.29 {ECO:0000256|ARBA:ARBA00012382};
GN ORFNames=PDE_01616 {ECO:0000313|EMBL:EPS26678.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26678.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26678.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC {ECO:0000256|RuleBase:RU004466}.
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DR EMBL; KB644409; EPS26678.1; -; Genomic_DNA.
DR AlphaFoldDB; S8ALE0; -.
DR STRING; 933388.S8ALE0; -.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_1_0_1; -.
DR OrthoDB; 25272at2759; -.
DR PhylomeDB; S8ALE0; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0042181; P:ketone biosynthetic process; IEA:UniProt.
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; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR12001:SF69; ALL TRANS-POLYPRENYL-DIPHOSPHATE SYNTHASE PDSS1; 1.
DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004466}.
SQ SEQUENCE 448 AA; 48813 MW; F9EF41A0F1A7B904 CRC64;
MRARTLSVTG LTLKRTPSIS VCPQCLRDDL YTTQSLLQTR NFRTGRRIDA SPFGAAATAA
QAIFKGLPRA PPGVSVDPLR MVGKELKFLS NNIRQLLGSG HPALDKVAKY YTRSEGKHMR
PLLVLLMSQA TAVDPRKDLS RTPNTAPVDI SLSPLSILED ANPDTDHLVP EPPKTQSFVG
DENILPNQRR LAEITELIHT ASLLHDDVID NAETRRGSAS ANIEFGNKMA VLAGDFLLGR
ASVALARLLD PQVIELMATV INNLVQGEFM QLKNTAKDEA KPVYTDNTVE YYLQKTYLKT
ASLISKSCRS AAVLGCSAPE VVEAAYAYGR NLGLAFQLVD DMLDYTLTEA ELGKPAGADL
ELGLATAPLL FAWKSNPELG PMVGRKFGKE GDVQRARELV YQSNGVEQTR ALAQDYADKA
VAAISDFPDS DAKAGLIEMA EKTMKRRK
//