PADC1_PHOAM
ID PADC1_PHOAM Reviewed; 1004 AA.
AC B2DBF0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Phyllocladan-16-alpha-ol synthase;
DE EC=4.2.3.45;
DE EC=5.5.1.12;
GN Name=PaDC1;
OS Phomopsis amygdali (Fusicoccum amygdali).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214568;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=N2;
RX PubMed=18391465; DOI=10.1271/bbb.70790;
RA Toyomasu T., Niida R., Kenmoku H., Kanno Y., Miura S., Nakano C.,
RA Shiono Y., Mitsuhashi W., Toshima H., Oikawa H., Hoshino T., Dairi T.,
RA Kato N., Sassa T.;
RT "Identification of diterpene biosynthetic gene clusters and functional
RT analysis of labdane-related diterpene cyclases in Phomopsis amygdali.";
RL Biosci. Biotechnol. Biochem. 72:1038-1047(2008).
CC -!- FUNCTION: Involved in the synthesis of labdane-related hydrocarbons by
CC catalyzing the conversion of geranylgeranyl diphosphate (GGDP) to
CC phyllocladan-16-alpha-ol in a two step via type B cyclization into a
CC (+)-copalyl diphosphate ((+)-CDP) intermediate.
CC {ECO:0000269|PubMed:18391465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:58756; EC=5.5.1.12;
CC Evidence={ECO:0000269|PubMed:18391465};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate + H2O = diphosphate + phyllocladan-
CC 16alpha-ol; Xref=Rhea:RHEA:26430, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:53643, ChEBI:CHEBI:58635; EC=4.2.3.45;
CC Evidence={ECO:0000269|PubMed:18391465};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- DOMAIN: The DXDD and DEXXE motifs are important for the catalytic
CC activity. {ECO:0000269|PubMed:18391465}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AB252834; BAG30961.1; -; mRNA.
DR AlphaFoldDB; B2DBF0; -.
DR SMR; B2DBF0; -.
DR KEGG; ag:BAG30961; -.
DR BioCyc; MetaCyc:MON-15022; -.
DR BRENDA; 4.2.3.45; 10693.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017057; Ent-kaurene_synthase_fun.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PIRSF; PIRSF036498; Ent-kaurene_synthase_fungi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Isomerase; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..1004
FT /note="Phyllocladan-16-alpha-ol synthase"
FT /id="PRO_0000415666"
FT MOTIF 321..324
FT /note="DXDD motif"
FT MOTIF 667..671
FT /note="DEXXE motif"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 667
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 667
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 671
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 671
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 872
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 876
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 880
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1004 AA; 112836 MW; 78D85416DEC79A5E CRC64;
MTIMDIDDHS RLRDLAVSLI RQAAEGYSPK YGYGSMSCAA YDTAWVSLVA KPFNGIKKWL
FPQSFKFLLE NQENDGSWGR QTSPVDRILN TAAPLLSLQR HAREPLQLHD VCEDGDLDDR
IHRATLSLQR QLSDWDIAST AHVGFEIIVP ALLNLLAAEG LCFSFKAQDE LMKVNAAKLK
RFDPEVLLYG KHKTTLLHSL EAFVGIIDFD KVVHHKVGGS FMASPSATAA YLMNASCWDD
EAEDYIKNVL VNGSGRGHGA VPSAYPSSNF EYSWLLSTLL HAGFTAKDIE CPELCDVAGM
LENSFIEGQG TIGFARSISS DADDTAKAAF ALNKLGYDVS VNEMVKEFEV KNHFQTYPSE
RDASLSANCN TLLALLHQKQ VGAYQPQILK CVKFLTRCWW NTDGPIRDKW NQSHLYSTML
MVQALTEFQA ILDQKGLPYG LNTVEMARVS ICLFQGCLRT MLQQCEDGSW SHSREQTAYA
VLTLGQARRL STFKHLQSQI DSAIDQAATF IRLHSVDLAQ QSLPEFIWTE KVSYTSPLVT
EAYCLAALKV ATSLVDNPGI VGESLDLGIP SRQRIDKYIW LFHQTPLFRS LPEWQLRASF
IEGHLFLPIV NEHRLDVFPR KNMDPDDDYI RLIPFTWTAT NNRNFTFASP AWLYDMIMVS
VVDYQADEFM EAVAGLTFSE DLSMLVGLIQ EVLTPYKTEP ASPVTSLIDM SSVQCPRAKL
SNIASGDIEE VRTCLRRFAS FFLDHPAVRN AQRDDRATAW REVHNYLVAH VRHTQDNMRL
NLQEQRRWYV SRNMPYFHWV RSNDDIACPI TFGFVTCLVP YLVANPTVER AVIGNESESI
VTSSDVSFDS VESKYYADDV CRHITNVTRI YNDCGSVVRD ATEKNLNSVN FPEFAVTASG
SEKQALRAMG EYERACCQAA FQRLEEASLQ TATTEAERAK RRRRLDVWKV FLDTADPYGQ
IYVVRDFTAR SVHVRETGIA STAKDVPLVS SSVPLVGGGP MLVT
