BTCA_COLOR
ID BTCA_COLOR Reviewed; 712 AA.
AC N4V6D4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Sesterterpene synthase btcA {ECO:0000303|Ref.3};
DE Short=TS {ECO:0000303|Ref.3};
DE AltName: Full=Betaestacins biosynthesis cluster protein A {ECO:0000303|Ref.3};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|Ref.3};
DE EC=4.2.3.- {ECO:0000269|Ref.3};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|Ref.3};
DE Short=GGDP synthase {ECO:0000303|Ref.3};
DE Short=GGS {ECO:0000303|Ref.3};
DE EC=2.5.1.29 {ECO:0000269|Ref.3};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase {ECO:0000303|Ref.3};
DE Short=GFDP synthase {ECO:0000303|Ref.3};
DE EC=2.5.1.81 {ECO:0000269|Ref.3};
GN Name=btcA {ECO:0000303|Ref.3}; ORFNames=Cob_11435, Cob_v004818;
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=30893003; DOI=10.1094/mpmi-12-18-0352-a;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, 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 (Ref.3). The bifunctional
CC terpene synthase btcA converts isopentenyl diphosphate (IPP) and
CC dimethylallyl diphosphate (DMAPP) into the sesterterpene betaestacin I
CC (Ref.3). The C-terminal prenyltransferase (PT) domain of btcA catalyzes
CC formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain
CC catalyzes the cyclization of GFPP into betaestacin I (Ref.3). The
CC cytochrome P450 monooxygenase btcB oxidizes the C25 methyl group of
CC betaestacin I to yield the carboxylic acid betaestacin IV via the
CC alcohol betaestacin III (Ref.3). The cytochrome P450 monooxygenase btcC
CC further catalyzes the multistep oxidation of betaestacin IV to produce
CC several compounds, including betaestacins Va, Vb, Vc and VI (Ref.3).
CC {ECO:0000269|Ref.3}.
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|Ref.3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|Ref.3};
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|Ref.3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|Ref.3};
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|Ref.3}.
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 -!- DISRUPTION PHENOTYPE: Does not affect growth and pigmentation on
CC plateculture, nor conidial formation. {ECO:0000269|Ref.3}.
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; KB726025; ENH79267.1; -; Genomic_DNA.
DR EMBL; AMCV02000011; TDZ21940.1; -; Genomic_DNA.
DR SMR; N4V6D4; -.
DR STRING; 1213857.N4V6D4; -.
DR EnsemblFungi; ENH79267; ENH79267; Cob_11435.
DR eggNOG; KOG0777; Eukaryota.
DR HOGENOM; CLU_014015_10_0_1; -.
DR OrthoDB; 981769at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
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; Reference proteome; Repeat; Transferase.
FT CHAIN 1..712
FT /note="Sesterterpene synthase btcA"
FT /id="PRO_0000453702"
FT REGION 1..332
FT /note="Terpene cyclase"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT REGION 333..706
FT /note="Prenyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT REGION 334..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..100
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT MOTIF 234..242
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT MOTIF 453..457
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:P9WEP0"
FT COMPBIAS 357..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 238..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 328..329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 414
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 417
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 446
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 462
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 463
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 540
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 541
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 580
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 587
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 597
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 607
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 712 AA; 81485 MW; 3B3397E0F31BFF50 CRC64;
MTTIWEHCVD VDGEVAASTG CFTTLPIRIH RRNDIADDAT KQSIHDWGAY VGDGWEQRSG
SSWSPVGNWG AFIFPESLPD RLGVITYLAN MGNIHDDLCD ELPFEEALKE HSNLSQAMEV
SNSDTRQCSK ASDRSMKMKK YISKCLLEAM EIDRARALRM INSYRSKWLD VMESQNVNDM
QTLEEYLAFR NLNGGMEAFW SMVEFGMAID ISESEKTHTR PLFQAAESAL VLTNDYWSWD
REWRLAQRTQ DPRIVNAVHL FMRTEGLSVD QAREKVRERI VDYEREYLRL KEEFYTQNPN
LPLYLRRYVE VCGVITAGNH YWCANCPRHH AWRDEESSPS ERSFSPSNEG IEDPRLSPGA
STTSSMSQKS SPATEITLSD VLGFMAINDN HKPQRSSDMA LMAPVQYIRS MPSKGLRSLM
VEALDQWLLV DDPELEQIKN IIDLLHNSSL ILDDIEDDSP LRRGLPATHT VFGQAQSINS
ANFMFVQAVQ MTQKLNNPAS LDTLLDELEC LFIGQSWDLY WKFHLQVPTE KEYLEMVDCK
TGAMFRLLAR LMFHESSVVS GTQVLQLLDE MCRLFGRFFQ IRDDFMNLYS TEYSDQKGFC
EDLDEGKMSY PLIMLLWQNP GQRDQIMGIF RQQASNTSRG PTSDRSRLPL ETKRYVMSLL
KGSDIMASTL RKLRDLEAAV DYSISGLEKA LGDANPVMRI VLSRLSVRDV SL
