ATR5_STAC4
ID ATR5_STAC4 Reviewed; 297 AA.
AC A0A084R1K6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Polyketide transferase ATR5 {ECO:0000305};
DE EC=2.3.-.- {ECO:0000305};
DE AltName: Full=Core atranone cluster (CAC) protein 5 {ECO:0000303|PubMed:25015739};
GN Name=ATR5 {ECO:0000303|PubMed:25015739}; ORFNames=S40285_03330;
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=IBT 40285;
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- FUNCTION: Polyketide transferase; part of the core atranone cluster
CC (CAC) which products are predicted to catalyze most or all steps of
CC atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP)
CC (PubMed:25015739). The initial cyclization of GGPP to dolabellane is
CC probably performed by the terpene cyclase ATR13 (PubMed:25015739). The
CC Baeyer-Villiger oxidation near the end of the atranone synthesis, which
CC converts atranones D and E to atranones F and G is predicted to be
CC catalyzed by the monooxygenase ATR8 (PubMed:25015739). Of the CAC's
CC other predicted gene products, the reducing PKS ATR6 might synthesize a
CC polyketide chain (PubMed:25015739). This polyketide is probably
CC transferred onto the atranone backbone by the polyketide transferase
CC ATR5 (By similarity). Other predicted CAC products include 4 oxygenases
CC (ATR2, ATR3, ATR4, and ATR14), 3 short-chain reductases (ATR7, ATR9,
CC and ATR10), and a methyltransferase (ATR12) (PubMed:25015739). These
CC may all be involved in the various steps of atranone biosynthesis,
CC although their specific roles must await experimental determination
CC (PubMed:25015739). {ECO:0000250|UniProtKB:Q4WAY4,
CC ECO:0000305|PubMed:25015739}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25015739}.
CC -!- SIMILARITY: Belongs to the polyketide transferase af380 family.
CC {ECO:0000305}.
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DR EMBL; KL659308; KFA70091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084R1K6; -.
DR SMR; A0A084R1K6; -.
DR STRING; 1283841.A0A084R1K6; -.
DR ESTHER; stac4-atr5; Thiohydrolase.
DR EnsemblFungi; KFA70091; KFA70091; S40285_03330.
DR HOGENOM; CLU_048587_1_1_1; -.
DR OMA; AQVRCFD; -.
DR OrthoDB; 990069at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="Polyketide transferase ATR5"
FT /id="PRO_0000442389"
FT REGION 49..272
FT /note="Abhydrolase domain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 297 AA; 33451 MW; B8E62E23FC062FB0 CRC64;
MAVMTREDVE FRTMDGLTLR GWLYPSGMRG PALVMTQGFN ASKEYLLADV AVWFQKRGVT
SLLVDIRTTG LSDGEPRNDI DLDKQVEDCH DAVSFLSRHP SVDPEMIVYW GYSLGAVISL
CAAALDKRAA AVIATAPNTD FIFDPVKRAA TLSLAMRDRL SRLAGNPPLY LKIIGEDGQN
PAGWYLGEER RSPEELDALF NSSNIMNQVT IQSYYRLLRW QPFGLMPSVS PTPVMIVTPS
DDDLSKPENQ RKLFDIFQEP KEFVLAENKG HMNCISGEDG EQFLQKQLEF MKRMLKF
