STTA_ASPTN
ID STTA_ASPTN Reviewed; 773 AA.
AC Q0CRW6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Preaspterpenacid I synthase sttA {ECO:0000303|PubMed:34085529};
DE Includes:
DE RecName: Full=Sesterterpenoid synthase {ECO:0000303|PubMed:34085529};
DE EC=4.2.3.- {ECO:0000269|PubMed:34085529};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase {ECO:0000303|PubMed:34085529};
DE Short=GFDP synthase {ECO:0000303|PubMed:34085529};
DE EC=2.5.1.- {ECO:0000269|PubMed:34085529};
DE AltName: Full=Aspterpenacid biosynthesis cluster protein sttA {ECO:0000303|PubMed:34085529};
DE AltName: Full=Ophiobolin family sesterterpenoid biosynthesis cluster protein A {ECO:0000303|PubMed:28604695};
GN Name=sttA {ECO:0000303|PubMed:28604695}; ORFNames=ATEG_03568;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=28604695; DOI=10.1038/nchembio.2408;
RA Clevenger K.D., Bok J.W., Ye R., Miley G.P., Verdan M.H., Velk T., Chen C.,
RA Yang K., Robey M.T., Gao P., Lamprecht M., Thomas P.M., Islam M.N.,
RA Palmer J.M., Wu C.C., Keller N.P., Kelleher N.L.;
RT "A scalable platform to identify fungal secondary metabolites and their
RT gene clusters.";
RL Nat. Chem. Biol. 13:895-901(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=34085529; DOI=10.1021/acs.orglett.1c01361;
RA Jiang L., Zhang X., Sato Y., Zhu G., Minami A., Zhang W., Ozaki T., Zhu B.,
RA Wang Z., Wang X., Lv K., Zhang J., Wang Y., Gao S., Liu C., Hsiang T.,
RA Zhang L., Oikawa H., Liu X.;
RT "Genome-based discovery of enantiomeric pentacyclic sesterterpenes
RT catalyzed by fungal bifunctional terpene synthases.";
RL Org. Lett. 23:4645-4650(2021).
CC -!- FUNCTION: Sesterterpenoid synthase; part of the gene cluster that
CC mediates the biosynthesis of aspterpenacids (PubMed:28604695,
CC PubMed:34085529). Performs both prenyl transferase and terpene cyclase
CC activity, converting isopentenyl diphosphate and dimethylallyl
CC diphosphate into geranylfarnesyl diphosphate (GFPP) and then converting
CC GFPP into preaspterpenacid I (PubMed:34085529). C22-oxidative
CC modification of preaspterpenacid I by the cytochrome P450 monooxygenase
CC sttB then leads to preaspterpenacid II. It has still to be determined
CC how preaspterpenacid II is further modified to produce aspterpenacids
CC (PubMed:34085529). {ECO:0000269|PubMed:28604695,
CC ECO:0000269|PubMed:34085529, ECO:0000305|PubMed:34085529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + 4 isopentenyl diphosphate =
CC (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate;
CC Xref=Rhea:RHEA:66860, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:128769;
CC Evidence={ECO:0000269|PubMed:34085529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66861;
CC Evidence={ECO:0000269|PubMed:34085529};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:28604695, ECO:0000269|PubMed:34085529}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of sesterterpenoid.
CC {ECO:0000269|PubMed:28604695}.
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; CH476597; EAU36842.1; -; Genomic_DNA.
DR RefSeq; XP_001212746.1; XM_001212746.1.
DR AlphaFoldDB; Q0CRW6; -.
DR SMR; Q0CRW6; -.
DR STRING; 341663.Q0CRW6; -.
DR EnsemblFungi; EAU36842; EAU36842; ATEG_03568.
DR GeneID; 4317926; -.
DR VEuPathDB; FungiDB:ATEG_03568; -.
DR eggNOG; KOG0777; Eukaryota.
DR HOGENOM; CLU_014015_10_0_1; -.
DR OrthoDB; 981769at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; -; 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.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..773
FT /note="Preaspterpenacid I synthase sttA"
FT /id="PRO_0000450607"
FT REGION 4..359
FT /note="Sesterterpenoid synthase"
FT /evidence="ECO:0000250|UniProtKB:C9K2Q3"
FT REGION 211..214
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 259..263
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 350..351
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 360..769
FT /note="Geranylfarnesyl diphosphate synthase"
FT /evidence="ECO:0000250|UniProtKB:C9K2Q3"
FT REGION 423..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 493
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 496
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 525
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
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 542
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 614
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 615
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 652
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 659
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 669
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 773 AA; 87735 MW; BFFEA3CF2499AA27 CRC64;
MDTISDVMKH CVPINYDDYD PLPADHFSTY PVFCSKATAE AIEASAEFTR KWKRACEVDG
LHQDKLNFQA CTTHLGHYNQ WAYPDCLPER VSLNAVLSDC AFFWDGMSPV TGRSTNVMIT
SPVDVSDSIS AEKMNELTQD FGIAMLSELQ SGRRIEPRFE INKMAVQVIR DFIAVDPFTG
IGHLKEWKGH LDAQEKSTHN NMSWEKYVEH RVNESGGNWG ISVGCWTNDI RISDEEKESV
KYLTQLACAG GILGNDYYSF PKEFDEHHRS GTLDRLQNGV ALLMREYGYT EEEAKEIIKK
EVIIREKKWM DGFDAWSRQA GPETGEIRRY LVMTMALMSG SMFWMSHAGR YHRTDLATTA
EDRATLIGKS RGALRVLAGY PPPKNLEGIV REPLASAVQD DNGHVQHKDA VADSSVRNGV
HHAFKKRNSR NGKQNGTEGS KSTFTNGNYV QPAKLQQHGT SINSMAIYTA PFQEAAGDIC
DAPYSYIDSL PSKKNRNKLL DLLNDWLQVP PSSLKRIKNI VHMLHNSSLM LDDIEDASAL
RRGQPATHTF YGISQTINSA NYVYVHAVHE VTRLYNPDAD ELRNLHRGQS LDLYWRHHAR
CPSMEEYIVM VDNKTGGLFR LMLRLMTAES SISRPLDTAL CRLLTLTGRY YQIRDDYLNL
ASADYESKKG FCEDFDEGKF SLPLIHLLSH TRYPDRITSA LFNRKPGTNL PYEMKRYILA
EMEEVQTLAY SQDVLKYLHE ELMHALDETE NRLGANDGIR MMLLGMGPKL LLC
