BTCA_NEOBT
ID BTCA_NEOBT Reviewed; 725 AA.
AC A0A2Z6FZ31;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Sesterterpene synthase btcA {ECO:0000303|PubMed:29185768};
DE Short=TS {ECO:0000303|PubMed:29185768};
DE AltName: Full=Betaestacins biosynthesis cluster protein A {ECO:0000303|PubMed:29185768};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:29185768};
DE EC=4.2.3.- {ECO:0000269|PubMed:29185768};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:29185768};
DE Short=GGDP synthase {ECO:0000303|PubMed:29185768};
DE Short=GGS {ECO:0000303|PubMed:29185768};
DE EC=2.5.1.29 {ECO:0000269|PubMed:29185768};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase {ECO:0000303|PubMed:29185768};
DE Short=GFDP synthase {ECO:0000303|PubMed:29185768};
DE EC=2.5.1.81 {ECO:0000269|PubMed:29185768};
GN Name=btcA {ECO:0000303|PubMed:29185768};
GN Synonyms=PbTS {ECO:0000303|PubMed:29185768};
OS Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Neocamarosporium.
OX NCBI_TaxID=1979465;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=PS-13;
RX PubMed=29185768; DOI=10.1021/acs.orglett.7b03418;
RA Narita K., Sato H., Minami A., Kudo K., Gao L., Liu C., Ozaki T.,
RA Kodama M., Lei X., Taniguchi T., Monde K., Yamazaki M., Uchiyama M.,
RA Oikawa H.;
RT "Focused genome mining of structurally related sesterterpenes: enzymatic
RT formation of enantiomeric and diastereomeric products.";
RL Org. Lett. 19:6696-6699(2017).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX DOI=10.1016/j.tetlet.2018.02.022;
RA Gao L., Narita K., Ozaki T., Kamukara N., Gan P., Minami A., Liu C.,
RA Lei X., Shirasu K., Oikawa H.;
RT "Identification of novel sesterterpenes by genome mining of phytopathogenic
RT fungi Phoma and Colletotrichum sp.";
RL Tetrahedron Lett. 59:1136-1139(2018).
CC -!- FUNCTION: Bifunctional terpene synthase; part of the gene cluster that
CC mediates the biosynthesis of betaestacins (PubMed:29185768, Ref.2). The
CC bifunctional terpene synthase btcA converts isopentenyl diphosphate
CC (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene
CC betaestacin I (PubMed:29185768, Ref.2). The C-terminal
CC prenyltransferase (PT) domain of btcA catalyzes formation of GFPP,
CC whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC cyclization of GFPP into betaestacin I (PubMed:29185768, Ref.2). The
CC cytochrome P450 monooxygenase btcB is then responsible for the six-step
CC oxidation of betaestacin I to yield betaestacin II (Ref.2). The roles
CC of the cytochrome P450 monooxygenase btcC and the alpha-ketoglutarate-
CC dependent dioxygenase btcD have not been identified yet (Probable).
CC {ECO:0000269|PubMed:29185768, ECO:0000269|Ref.2, ECO:0000305|Ref.2}.
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:0000269|PubMed:29185768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:29185768};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81; Evidence={ECO:0000269|PubMed:29185768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:29185768};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WEV7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29185768}.
CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}.
CC -!- DOMAIN: The conserved DDXXD motifs as well as the NSE/DTE motif are
CC important for the catalytic activity, presumably through binding to
CC Mg(2+). {ECO:0000250|UniProtKB:P9WEP0}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase
CC family. {ECO:0000305}.
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DR EMBL; LC274619; BBE36502.1; -; Genomic_DNA.
DR SMR; A0A2Z6FZ31; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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; -; 2.
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; 2.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Repeat; Transferase.
FT CHAIN 1..725
FT /note="Sesterterpene synthase btcA"
FT /id="PRO_0000453701"
FT REGION 1..333
FT /note="Terpene cyclase"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT REGION 334..722
FT /note="Prenyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT REGION 352..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..104
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT MOTIF 236..244
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT MOTIF 481..485
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT COMPBIAS 352..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 240..244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 442
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 445
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 474
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 490
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 491
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 568
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 569
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 604
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 611
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 621
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 631
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 725 AA; 82104 MW; B6D8DC6660CE39E7 CRC64;
MANPPVTEWK QSEAIPAHVA QETGCFTTLP IRIHKNNSIA DQATLESIND WKQHLDDGWE
SRSGSAISKV GNWCSFIFSE ALPERLPCIT YLANIGNIHD DATEDATLDE AITSHAQFST
ALSLDTDDEP SLQEAKTRRF RHLVSNCVLE ILSIDRDMGT RMIVSYQKKW LDVMEHLNYE
GIESLEEYLE FRMLNGGMEP FWLMCQFGMG LNIPDAELAP TRHIFEPAEW ALVLTNDYWS
WGREYNASLT KGSRIVNSIE LLSRLRNISY DEAKEVVRDL ITTYEAEYER RVQDFLRENP
STQMYLRQFI EVAGLVVAGN HYWCANCPRH HAWKEQDQAV HAVDQLEEFP AVEAQSPSSA
THTAAPQEDP PVTEAPSPIS SPSSSSSAKP SSSSAADSSS CTSTSQHSPS ETDSTPPSSL
HLLKSPHPVD APCTYMSSLP SKGVRSTLIH ALNQWFQISS RNVTLIKEIT SMLHNSSLIL
DDIQDQSPLR RGKPAAHTIF STAQSINSST YLFVRAMQMV SENFESSVQM SFLEILQRMH
IGQSYDLHWR FHLQCPTEDE YFEMVDAKTG CMFEMLLLLM SSKSRHVKDH SFTSFIRTFG
RYFQVRDDYM NLTSGEYTAG KGWCEDLDEG KLSYPLIECQ KMAPASFTQI MGIFRAKQAD
TAQLSDETKK YVIELFRKSG VLDSTLDWIM EMERQLLMEV KRLEGVMGDS NPMLYVLLQT
LSLNQ
