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AUSV_ASPCI
ID   AUSV_ASPCI              Reviewed;        2531 AA.
AC   A0A0U5GK88;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Highly reducing polyketide synthase ausV {ECO:0000303|PubMed:28233494};
DE            EC=2.3.1.- {ECO:0000269|PubMed:28233494};
DE   AltName: Full=Austinoid biosynthesis cluster protein V {ECO:0000303|PubMed:28233494};
GN   Name=ausV {ECO:0000303|PubMed:28233494}; ORFNames=ASPCAL14365;
OS   Aspergillus calidoustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=454130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF006504;
RX   PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA   Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA   Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT   "Draft genome sequences of fungus Aspergillus calidoustus.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=28233494; DOI=10.1021/acschembio.7b00003;
RA   Valiante V., Mattern D.J., Schueffler A., Horn F., Walther G.,
RA   Scherlach K., Petzke L., Dickhaut J., Guthke R., Hertweck C., Nett M.,
RA   Thines E., Brakhage A.A.;
RT   "Discovery of an Extended Austinoid Biosynthetic Pathway in Aspergillus
RT   calidoustus.";
RL   ACS Chem. Biol. 12:1227-1234(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=29076725; DOI=10.1021/acschembio.7b00814;
RA   Mattern D.J., Valiante V., Horn F., Petzke L., Brakhage A.A.;
RT   "Rewiring of the austinoid biosynthetic pathway in filamentous fungi.";
RL   ACS Chem. Biol. 12:2927-2933(2017).
CC   -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of calidodehydroaustin, a fungal
CC       meroterpenoid (PubMed:28233494, PubMed:29076725). The first step of the
CC       pathway is the synthesis of 3,5-dimethylorsellinic acid by the
CC       polyketide synthase ausA (PubMed:28233494). 3,5-dimethylorsellinic acid
CC       is then prenylated by the polyprenyl transferase ausN
CC       (PubMed:28233494). Further epoxidation by the FAD-dependent
CC       monooxygenase ausM and cyclization by the probable terpene cyclase ausL
CC       lead to the formation of protoaustinoid A (By similarity).
CC       Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by
CC       the combined action of the FAD-binding monooxygenases ausB and ausC,
CC       and the dioxygenase ausE (By similarity). Acid-catalyzed keto-
CC       rearrangement and ring contraction of the tetraketide portion of
CC       preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (By
CC       similarity). The aldo-keto reductase ausK, with the help of ausH, is
CC       involved in the next step by transforming preaustinoid A4 into
CC       isoaustinone which is in turn hydroxylated by the P450 monooxygenase
CC       ausI to form austinolide (By similarity). The cytochrome P450
CC       monooxygenase ausG modifies austinolide to austinol (By similarity).
CC       Austinol is further acetylated to austin by the O-acetyltransferase
CC       ausP, which spontaneously changes to dehydroaustin (PubMed:28233494).
CC       The cytochrome P450 monooxygenase ausR then converts dehydroaustin is
CC       into 7-dehydrodehydroaustin (PubMed:28233494). The hydroxylation
CC       catalyzed by ausR permits the O-acetyltransferase ausQ to add an
CC       additional acetyl group to the molecule, leading to the formation of
CC       acetoxydehydroaustin (PubMed:28233494). The short chain dehydrogenase
CC       ausT catalyzes the reduction of the double bond present between carbon
CC       atoms 1 and 2 to convert 7-dehydrodehydroaustin into 1,2-dihydro-7-
CC       hydroxydehydroaustin (PubMed:28233494). AusQ catalyzes not only an
CC       acetylation reaction but also the addition of the PKS ausV diketide
CC       product to 1,2-dihydro-7-hydroxydehydroaustin, forming
CC       precalidodehydroaustin (PubMed:28233494). Finally, the iron/alpha-
CC       ketoglutarate-dependent dioxygenase converts precalidodehydroaustin
CC       into calidodehydroaustin (PubMed:28233494).
CC       {ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000269|PubMed:28233494,
CC       ECO:0000269|PubMed:29076725}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:28233494}.
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:0000250|UniProtKB:Q5KTM9}.
CC   -!- MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a
CC       contiguous DNA region, while clusters from E.nidulans and P.brasilianum
CC       are split in their respective genomes. Genetic rearrangements provoked
CC       variability among the clusters and E.nidulans produces the least number
CC       of austionoid derivatives with the end products austinol and
CC       dehydroaustinol, while P.brasilianum can produce until
CC       acetoxydehydroaustin, and A.calidoustus produces the highest number of
CC       identified derivatives. {ECO:0000305|PubMed:29076725}.
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DR   EMBL; CDMC01000024; CEL11262.1; -; Genomic_DNA.
DR   SMR; A0A0U5GK88; -.
DR   STRING; 454130.A0A0U5GK88; -.
DR   EnsemblFungi; CEL11262; CEL11262; ASPCAL14365.
DR   OrthoDB; 19161at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000054771; 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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR011032; GroES-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 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; 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; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 3.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..2531
FT                   /note="Highly reducing polyketide synthase ausV"
FT                   /id="PRO_0000453870"
FT   DOMAIN          2444..2521
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          10..435
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q5KTM9, ECO:0000255"
FT   REGION          554..882
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q5KTM9, ECO:0000255"
FT   REGION          940..1236
FT                   /note="Dehydrogenase (DH) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q5KTM9, ECO:0000255"
FT   REGION          1414..1592
FT                   /note="Methyltransferase (CMet) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q5KTM9, ECO:0000255"
FT   REGION          1832..2133
FT                   /note="Enoyl reductase (ER) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q5KTM9, ECO:0000255"
FT   REGION          2156..2331
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q5KTM9, ECO:0000255"
FT   ACT_SITE        180
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        644
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        971
FT                   /note="For beta-hydroxyacyl dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2481
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2531 AA;  275891 MW;  D0A9F5922ECBC3F3 CRC64;
     MAGTDSSTPI AIIGLSGRFP GEASNPQKLW SVLMNKQSTR SEVPPDRFNV NAFYHPSGSR
     AGTVNTRWGH FMTRDPAAFD APFFSVLPEE ARAMDPQSRM ALECAFEAFE NAGMTMDAVA
     GTRTACYVAS FTHDYAELLA QDGESQPRYK FTGCGAGMLA NRISWFFDLQ APSVTVDTAC
     SSSLVALHLG CQSIHTGDAD MVLVGGANVI LSPQMMASQS SLGFLSPDGR SKAFDEQADG
     YARGEGVGFL LLKPLGAALA DGDAIRAVIR GTGVNQDGRT AGITVPSAQA QERLIRSVYD
     RACLDPVETP FVEAHGTGTR KGDLAEASSL ASVFCHRRLP QNPLYIGSVK TNIGHLEAAA
     GVAQVIKTVL ALENGIIPPN IWFTRPSTAL PLDRWRLKVP VEPVSWPEGE KRRASINSFG
     YGGTNAHCVM ETLEEYSMGQ GAAKAGTLCQ EPRCNHEARP REEEAPMLIF WSSHDKGGIS
     RLAAQYAQYL EAKVKSATDR SSLTRRLCMT LHSRRSVMPW KSYIVSHSAN SIVESFRNGA
     AQPLRSSEPP AIVFVFTGQG AQWPGMGRQL IRYPEYLESL QLAGRFLQCL GLQVSVIDEI
     KATPEQSSLA SPEVSQTLCT VLQVALVDLL ESFGINPTAV IGHSGGEIAA AYAKGAISRE
     AAWTIAFHRG RLCSSLPDYA PSLQGGMLVA GLGREDCATY IGRLTEGVAV IACVNSPLSC
     TVAGDLSALD QLEGLLSEAG CFHRRLRVSR AYHSPHMQVI AGECYKAISS ARPLADTEKS
     LNTTMYSTVT RGVVECSDLG PDYWVSNMIE PVEFVGAVES VIRDLGNRTA PTVFVEIGPH
     SALQGPLRQI LDAASSAERF PYTSLLVRGR DAHHTLLESM GSLIQHGCHL KLHEINQLST
     EEGFLVNLPP YPWNHDERNR YWAESSVSRK RRFRQHARHD LCGIRVEDDL PGEATWRNIL
     SPSENPWILD HRVQGTIVYP AAGMLTAVVE AVRESVRNVL EISYFELRDV KISRPIVFSS
     EEDVVHTRLR LRQETGQCPG SFEFQHYSEK GDGWELNCSG SVLAGTPSDS PDAAHRTRYA
     HCRAASYVET TPRQAYSQWA SVGLQFGRWF QNLTQLSKGP SSAIGTVRIP STTDCMPCGF
     EQDMLVHPVV LDALVQLGLS TSKEEYEEPH DTMVPVAFSR VHISADIPQG PGTEMVGYSV
     INDSASGVNV AASDTQWAQP WIILDGLELA TLSVRSGDAV GPTAARVPRK LAAATEWLPS
     IIHTPGDIIQ RACNLPGESM QADRACELQW AALIWIQRIL RGCPLTDVSP SPPHLRRLHH
     GMTRLYNSAI QGDSFPEDSR LKMLLSSPRK VQDEALQQVA NSSIDGEILD HHCRMLDRIL
     RGNMHSIEAL LEESRLHRWY AEGITWRANH DKVSSYLRLH ARNNAQAQIL EIGGGTGGLT
     LSALRAMTLS DGSALFDSYC FTDISGGFFE KARKKFAAWA HCMSFVTLNI EHDLERQGFG
     EAQFDLILAD NVLHATKSIR HTLSAVRKLL KPTGRLVLSE ITRNMPHITM TVGALEGWWL
     GVEDGRVWEP TLSVEQWDGA LRDTGFSGVD ISLHDRPKGD HIMTGMVATA RQLGLTPPPT
     PAVIIIHMHN LTPRVRTFVT GCITQLRALG MDVAVESLGS SSAHDNLHDK TVVLLLDADP
     EQRDLATINE TEWTALKHTL LSCADAVWIT RGANADGWNP WASMAQGLVR SLRAENPATA
     ITMVDIACEQ DLDSATTISS ITRLALAGRR AKITHESHDW EYCIRGREIL IPRVMTEDGV
     NGAVFKSVKS ETEQIPFGQP GTSVALTTIE PLRFVQDPAY WLEPLGKDEA EVATRATHLV
     SSQGQNNSSH GLVTVCGTVT RLGTACHSEL SVGDRVMTIQ RGAIRNLYRC PLTLCHRIPE
     KLGDFGVAVR VLWAYTTAFY CLVHKASLKA GEAVLIDCAS NTLQESLIRL AQHARAEVFL
     LVSSEARKNQ LASTFLVPPD HILSTGGEGL QGLDMGRRFD LILLDAAPTN LLQQYLAPGA
     RLVLVQHQGR TQHSSFHGSN GSVDRHESWF LDSKGTRLRL PIPGDARMYT IAPDTLSHED
     RTIVAQILRH VTELVRSQEI HADSGGAKPG CSRSEESLHI TNCVEGAPNQ LVVEAHGRAL
     VPDFHNKVIK SRPTAHLLPN ATYIIAGGSG GLGASLARWM CHRGARHIVI LSRQADTRPG
     VAKLIEDLAV NGVKVAAVPC DITDSQQDSV FHNMSFGAWN RAIHPKVMGS WNLHTHCPSE
     VDFFILLSSF VGTVGLRGQA NYAAGNSFQD ALAHHRRSRG QAGVSLSLGF IDGAGFIAQS
     SGRVAENVSK FNFLHIQQSE FLQLVELAVT SPDRLPAQVI TGCGTGGMVA AREGDPGDVY
     WLRDPRFQLL AQVDLHHFQR MNSEPAAEGF SLGALLAAAE TVGAAATAVL DALCRKLATA
     ASIEAGDIDT SRQLSSYGVD SLLAVDLRAY LATEARLDIS VFELMRSRPM RELARDLALR
     SKYFRSSHVA T
 
 
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