PBCB_EMENI
ID PBCB_EMENI Reviewed; 397 AA.
AC A0A1U8QLG8; C8VN85; Q5BCY8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase AN1592 {ECO:0000303|PubMed:22506079};
DE Short=GGPP synthase {ECO:0000305};
DE Short=GGPPSase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000305|PubMed:22506079};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.1 {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Farnesyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.29 {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Geranyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.10 {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Pimaradiene biosynthesis cluster protein AN1592 {ECO:0000303|PubMed:22506079};
GN ORFNames=AN1592, ANIA_01592;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=22506079; DOI=10.1371/journal.pone.0035450;
RA Bromann K., Toivari M., Viljanen K., Vuoristo A., Ruohonen L.,
RA Nakari-Setaelae T.;
RT "Identification and characterization of a novel diterpene gene cluster in
RT Aspergillus nidulans.";
RL PLoS ONE 7:e35450-e35450(2012).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=27098256; DOI=10.1007/s00253-016-7517-5;
RA Bromann K., Toivari M., Viljanen K., Ruohonen L., Nakari-Setaelae T.;
RT "Engineering Aspergillus nidulans for heterologous ent-kaurene and gamma-
RT terpinene production.";
RL Appl. Microbiol. Biotechnol. 100:6345-6359(2016).
CC -!- FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene
CC cluster that mediates the biosynthesis of the diterpene ent-pimara-
CC 8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the
CC cluster, the HMG-CoA reductase AN1593 functions in the mevalonate
CC pathway, which produces isoprenoid precursors (PubMed:22506079,
CC PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase
CC AN1592 is needed in the formation of GGPP, the precursor for diterpenes
CC (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase
CC pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-
CC 8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles
CC of the remaining cluster enzymes in ent-pimara-8(14),15-diene
CC biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase
CC AN1598, the glutathione S-transferase AN1595, the oxidoreductases
CC AN1596 and AN1597 probably function as decorative enzymes (Probable).
CC It is possible that in biological conditions the compound is oxidized
CC to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene
CC compound predominant in many plant extracts (Probable).
CC {ECO:0000269|PubMed:22506079, ECO:0000269|PubMed:27098256,
CC ECO:0000305|PubMed:22506079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:22506079}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pbcR. {ECO:0000269|PubMed:22506079,
CC ECO:0000269|PubMed:27098256}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AACD01000025; EAA64299.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85177.1; -; Genomic_DNA.
DR RefSeq; XP_659196.1; XM_654104.1.
DR AlphaFoldDB; A0A1U8QLG8; -.
DR SMR; A0A1U8QLG8; -.
DR STRING; 162425.CADANIAP00008225; -.
DR EnsemblFungi; CBF85177; CBF85177; ANIA_01592.
DR EnsemblFungi; EAA64299; EAA64299; AN1592.2.
DR GeneID; 2875291; -.
DR KEGG; ani:AN1592.2; -.
DR VEuPathDB; FungiDB:AN1592; -.
DR eggNOG; KOG0777; Eukaryota.
DR HOGENOM; CLU_014015_6_0_1; -.
DR OMA; RTITMAH; -.
DR OrthoDB; 981769at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 2: Evidence at transcript level;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..397
FT /note="Geranylgeranyl pyrophosphate synthase AN1592"
FT /id="PRO_0000450840"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 123
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 152
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 168
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 169
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 247
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 248
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 281
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 288
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 298
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 308
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT SITE 191
FT /note="Important for determining product chain length"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 397 AA; 45185 MW; 46E5E26D2E851FA6 CRC64;
MSPPLDSALE PLSEYKETAF PRTEKDPSQY KEHDLVTPEK EIQTGYFSPR GSHSSHGSHD
SSASSNISLD DARMSDVNNS PNVFHDDPDT IDEKLSMYWK AANETVIREP YDYIAGIPGK
EIRRKLLEAF NHWYKVDEQS CQAIATTVGM AHNASLLIDD IQDSSKLRRG VPCAHEVFGI
AQTINSANYV YFLAQNQLFR LRSWPQAISV FNEEMVNLHR GQGMELFWRD NLLPPSMDDY
LQMIANKTGG LFRMIVRLLQ TSSRQVIDVE QLVDVLGLYF QILDDYKNIR EEKMAAQKGF
FEDLTEGKFS FPICHAIGEG AKNRTALLHM LRLKTDDMKI KQEAVCILDN AGSLDYTREV
LYGLDRKARS LLREFKTPNP FMEALLDAML SSLQACH
