VDTX1_BYSSP
ID VDTX1_BYSSP Reviewed; 2193 AA.
AC A0A443HK66;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Highly reducing polyketide synthase VdtX {ECO:0000303|PubMed:31304040};
DE Short=HR-PKS VdtX {ECO:0000303|PubMed:31304040};
DE EC=2.3.1.- {ECO:0000303|PubMed:31304040};
DE AltName: Full=Viriditoxin biosynthesis cluster protein X {ECO:0000303|PubMed:31304040};
GN Name=VdtX {ECO:0000303|PubMed:31304040}; ORFNames=C8Q69DRAFT_515060;
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075;
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Maekelae M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
RN [2]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31304040; DOI=10.1186/s40694-019-0072-y;
RA Urquhart A.S., Hu J., Chooi Y.H., Idnurm A.;
RT "The fungal gene cluster for biosynthesis of the antibacterial agent
RT viriditoxin.";
RL Fungal Biol. Biotechnol. 6:2-2(2019).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of viriditoxin, one of the 'classical'
CC secondary metabolites produced by fungi and that has antibacterial
CC activity (PubMed:31304040). The first step is performed by the
CC polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-
CC CoA units to form the heptaketide monomer backbone of viriditoxin
CC (PubMed:31304040). The product of VdtA is then O-methylated on C7 by
CC the O-methyltransferase VdtC. The O-methyl group is important for the
CC stereoselective coupling of the monomers at the final step of
CC viriditoxin biosynthesis (PubMed:31304040). The short-chain
CC dehydrogenase/reductase VdtF is involved in the reduction of the C3-C4
CC double bond (PubMed:31304040). The FAD-binding monooxygenase VdtE then
CC converts the ketone group into a methyl-ester group to yield semi-
CC viriditoxin (PubMed:31304040). Finally, the laccase VdtB is involved in
CC dimerization of 2 semi-viriditoxin molecules to yield the final
CC viriditoxin. The non-catalytic carboxylesterase-like protein VdtD
CC affects the stereochemistical outcome of the coupling
CC (PubMed:31304040). The highly reducing polyketide synthase VdtX is not
CC involved in viriditoxin synthesis, but might possibly play a role in
CC the production of additional metabolites not identified yet
CC (PubMed:31304040). {ECO:0000269|PubMed:31304040}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC (CMeT) domain responsible for the incorporation of methyl groups; an
CC enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:31304040}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of viriditoxin.
CC {ECO:0000269|PubMed:31304040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCNU01000014; RWQ92174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HK66; -.
DR SMR; A0A443HK66; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2193
FT /note="Highly reducing polyketide synthase VdtX"
FT /id="PRO_0000448342"
FT DOMAIN 2102..2183
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..420
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 513..809
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 877..1128
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1256..1390
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 1575..1783
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 1807..1981
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2143
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2193 AA; 240602 MW; 59E0F629D99E78B1 CRC64;
MAICGIAVRL PGGISNDAQL WDFLLAKRDA RSQVPGSRYN ISGYHSDSGK HGTSKSKYGY
FLDESVDLGT LDTSFFSFTK LELEYIDPCQ RQLLEVVREC FESAGEVNYR GKDIGCFVGS
FGDDWTENLT HDEQTSAKYP LMVGGDFATP NRVSYEYNLH GPSVSIRTAC SSSLVALHSA
CLSIQNGDCS AAIVAGFNLI LTPTMTMIMS SKGVLSADGS SKSFDADADG YGRGEAVNAV
YIKPLHDAIR DGNPIRAVIR GTATNSDGKS AGFTVPSADA QEDVIRKAYK AAGISDLSQT
AFVECHGTGT TVGDPIEVAA IANTFGGDMY IGSVKPNVGH SEGASGLTSL IKAVLAVENR
TIPPNIKFNT PNPKIPFEAK KITVPVEATP WPWNRCVRAS VNSFGMGGVN AHVIIESADN
FTPPTSEVIE EHDSTPQLLL FSANTQDSLE AMIQRNLAYL RENTDSLRDL VYTMGARREH
LSFRAASIVH SDMSVTTASF GKAPSSPPDI VMVFAGQGAQ WPGMGVELFK SNATFRRSIL
EMDSVLQSLP DAPAWSIADE ISKEHQTSML YLSSYSQPIC TALQVALVNT LFELNIRPYA
VIGHSSGELA AAYAAGRLTA SQAVTLAYYR GIVAGKVAQA GYYPFLRPGV VVACENSPSS
VTISGDIDQV QYVMQEISLA HPEILCRQIK SDTAYHSHHM KSVGDTYHSF INPFFRGETE
VNCQPVHFFS TVTGDELSDG DHVGPKYWQQ NLESRVLFQG ALENIISRQR SRHLLFLDVS
PHSTLAGPIR QTLEQAEVAH PYVPCLIRFK NCAESFLSTI GQLYSHRQPL DFNMLTNPDR
TAKVLTDVPT YPWQHGYSNL YTTRQNNEWL FRKQPKHELL GTRVVDSTDN EPCWRNVLYL
EHVTWLRDHK VSGNIVFPAA GYVMMAGEAV RQIGSTASGF IVRQMVLDTA MVLNQSNPTE
IVTSLRKHRR DRWYSFTISS HNGVKWIEHC YGEVAQENLS RDINVSNWYK TLSRGGVEFG
PAFQCVESQS CSVTSNTVSG RIVSKLDSVL HIVYGAIYKG FDWQVESLPV PTSIGEIMIG
ECVSDLDVTM WADVSRNSNI LVNGEAFGSD GCLLIRIKDI VLRPLGANQA CFEEDESHAG
ARLLWKPSMQ FLNLADLIQT PVNWTKQTML LNDFTSLCIE RALCLLHAQG DWLQRQPKPS
SEQSMESLVE KILATSAAPC ARAMIKVLDN IVPICKGEID ALEVLMGDDT LYELYNYLNE
PQQRILEIGA GTGGTTAKIL PRTKYSTYTF TDISAAFFPA AKDRFQCHAN VVYRTLDITK
DPLDQANVLH ATPNLYETLS NLLLEELCGD AKFTNFIVGV LPGWWAGESD GRADEPYISP
DRWDSILKAA APPLHSLAFM LASPSCVPES PLKRNVTLLS DVTSSEIAVR MQKQLLSRGY
SVGVQSLDQS LMDGEDVIIL VDTVSPFFHN LDSRKLSTFQ NLLRELQRSH SGALWVTRSI
QIDCRDPRYS PTLGVARTVR SEFGLDFGTC EVDTLKYTSI GLVIDVFEAF HGRRHGQNAY
PEYEYAIRED TADAGQQVQL LGDDEVELQV DTAGVNFLTV LINSASDGVG LAAIQISKMI
GATIYATVIG EDKVEYLTAS HGIPRDHIFN SRDSSFLDGI MRVTNGRGVD LVLTSLSADF
IQASCDCVAN FGKLVNLSKP TAANQGQFPI DSFHPNMSYA SVDIIDYIKR RPKESKRLLE
EIVELYKQGH IQPITPVKTF TATDIRQCFD YMQSGQHIGQ LRLSLKSQDT FIEAVCSPKT
MIFQSDASYL LVGGLGGLGA EIARWMAEHG ARNLIFLSRS ADAESNIRLF RELESQGCSV
QAIKGSVCNA SDVKRAISAA RIKLKGIFNM SMVLQDASLL KMSSDEWNAA TGPKIQGTWN
LHDASLDQDL DFFLLFSSMG GILGIPGQAN YASANTFMDA FVQFRHSSHL PASVIDIGEV
QGIGHVANNP EILNRLKLLE CARMSQKDLF HAITIAISHS LPPQTLDYSR YENPAQFITG
LRDTTGMLDS TGGKSMLLDS RLAAYVGNSA AVTAPTETKT SANKLNNFVS SAATDSAILS
EPSATQFVSL EIARWVFDLL MKPVDDDSEI DLSRSLVDVG LDSLAAVEMR SWLKSSLGLD
ISVLEIMASP SLAAMGEHVI RELVRKFGGD NKN
