ID SORA_PENRW Reviewed; 2581 AA.
AC B6HNK3;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Highly reducing polyketide synthase sorA {ECO:0000303|PubMed:25580210};
DE Short=HR-PKS sorBA {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:25580210};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein A {ECO:0000303|PubMed:25580210};
GN Name=sorA {ECO:0000303|PubMed:25580210};
GN Synonyms=pks13 {ECO:0000303|PubMed:27107123}; ORFNames=Pc21g05080;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION.
RX PubMed=25580210; DOI=10.1039/c3sc52911h;
RA Fahad A.A., Abood A., Fisch K.M., Osipow A., Davison J., Avramovic M.,
RA Butts C.P., Piel J., Simpson T.J., Cox R.J.;
RT "Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis.";
RL Chem. Sci. 5:523-527(2014).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DOMAIN.
RX PubMed=27107123; DOI=10.1128/aem.00350-16;
RA Salo O., Guzman-Chavez F., Ries M.I., Lankhorst P.P., Bovenberg R.A.,
RA Vreeken R.J., Driessen A.J.;
RT "Identification of a polyketide synthase involved in sorbicillin
RT biosynthesis by Penicillium chrysogenum.";
RL Appl. Environ. Microbiol. 82:3971-3978(2016).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28618182; DOI=10.1111/1751-7915.12736;
RA Guzman-Chavez F., Salo O., Nygaard Y., Lankhorst P.P., Bovenberg R.A.L.,
RA Driessen A.J.M.;
RT "Mechanism and regulation of sorbicillin biosynthesis by Penicillium
RT chrysogenum.";
RL Microb. Biotechnol. 10:958-968(2017).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of sorbicillinoids, a diverse group of
CC yellow secondary metabolites that restrict growth of competing
CC pathogenic fungi but not of bacteria (PubMed:25580210, PubMed:27107123,
CC PubMed:28618182). Sorbicillinoids biosynthesis requires the action of
CC two PKSs (PubMed:25580210). SorA iteratively combines three acetyl
CC units and the growing chain is modified by the ketoacyl reductase
CC subunit, and optional by the enoyl reductase subunit in the second
CC cycle (PubMed:25580210). The polyketide is then handed over to the PKS
CC SorB, which adds three more acetyl units, and two methyl groups
CC (PubMed:25580210). SorB releases an aldehyde, which undergoes
CC spontaneous cyclization resulting in the formation of sorbicillin or
CC 2',3'-dihydrosorbicillin (PubMed:25580210). The monooxygenase sorC
CC oxidizes sorbicillin and 2',3'-dihydrosorbicillin to 2',3'-
CC dihydrosorbicillinol and sorbicillinol, respectively (PubMed:28618182).
CC The oxidoreductase sorD further converts sorbicillinol into
CC oxosorbicillinol (PubMed:28618182). Sorbicillinol is the building block
CC for the other sorbicillinoids such as disorbicillinol, bisvertinolon,
CC and dihydrobisvertinolone (By similarity).
CC {ECO:0000250|UniProtKB:G0R6S8, ECO:0000269|PubMed:25580210,
CC ECO:0000269|PubMed:27107123, ECO:0000269|PubMed:28618182}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25580210, ECO:0000269|PubMed:27107123,
CC ECO:0000269|PubMed:28618182}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of sorbicillinol
CC (PubMed:27107123, PubMed:28618182). {ECO:0000269|PubMed:27107123,
CC ECO:0000269|PubMed:28618182}.
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; AM920436; CAP95405.1; -; Genomic_DNA.
DR RefSeq; XP_002567554.1; XM_002567508.1.
DR AlphaFoldDB; B6HNK3; -.
DR SMR; B6HNK3; -.
DR STRING; 500485.B6HNK3; -.
DR GeneID; 8313805; -.
DR KEGG; pcs:Pc21g05080; -.
DR VEuPathDB; FungiDB:PCH_Pc21g05080; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; STPICVA; -.
DR OrthoDB; 5396558at2759; -.
DR BioCyc; PCHR:PC21G05080-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c21.
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:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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 PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 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; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2581
FT /note="Highly reducing polyketide synthase sorA"
FT /id="PRO_0000443834"
FT DOMAIN 14..436
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT ECO:0000305|PubMed:27107123"
FT DOMAIN 966..1273
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2497..2574
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:27107123"
FT REGION 574..868
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27107123"
FT REGION 966..1270
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27107123"
FT REGION 966..1103
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1119..1273
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1461..1568
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27107123"
FT REGION 1873..2184
FT /note="Enoyl reductase (ER)domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27107123"
FT REGION 2207..2389
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27107123"
FT ACT_SITE 187
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 322
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 359
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 998
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1184
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2534
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2581 AA; 279283 MW; 21297AC62F722936 CRC64;
MGSIDNTARG SSASEPIAII GMSAKFAGDA TNTDNLWRML IEGRSGWSPF PDSRFRSEGV
YHPNNERLNS THVKGAHFLA EDVGLFDAAF FGYSGETAAS MDPQYRLQLE SVYEALENAG
LPLTKIAGSN TSVFTGVFVH DYRDGFLRDA DNLPRLMATG TGVPMMANRV SHFFDLRGAS
MTIETACSSG MVAVHQAVQS LRTGEADMSI VGGANLTLNP DMFKALGSAG FLSADGKSYA
FDSRASGYGR GEGVGTLVVK RLSDALAAGD PIRAVIRESM LNQDGKTETI TSPSLEAQEA
LVRGCYQKAG LDPRETQYFE AHGTGTQAGD TIEAQGIATV FASRQEPLLI GSIKTNVGHT
EAASGLASII KTALAMENGV IPPSINFEKP NPKISLDDWN LKLVREVETW PAGPIRRASI
NNFGYGGSNA HIILEDSASW VKAIGGQNGR TNGFADGHSN GPNANGHHST LDPHVQESQV
ISKVLVLSGK DKQACEKMTA NLADYLRQTQ STNSNPRELL DSLIYTLGQR RSRFPWVVAH
PIPVTEGYET VVQTLQSPKF KPTRTSRRPR IGMVFTGQGA QWNAMGRELI EAYPVFKASL
QEAAGYLEQF GAEWSLMDEL MRDAEKSRIN EVGLSTPICV AVQISLVRLL RAWGIVPVAV
TSHSSGEIAA AYSAGAVSYK TAMAFSYYRA VLAADKSLRG PVKGGMIAVG LGLEETESYL
RRLSSEGQAA IACINSPSSI TVSGDLSAVV ELEDLANADG VFARRLKVDT AWHSHHMTPI
ANVYCEALEN TRAEKIDRDA LTTVAFSSPV TGGRITDAQQ IARPEHWVES LVQPVQFVAA
FTDMVLGGSG SVGSNVDVVV EVGPHTALGG PIQEILGLPE FKDLNIPYYG TLVRKLDARD
SMHALASSLL REGYPVNMGA VNFAHGRGQY VKVLTNLPSY PWNHQAKHWA EPRLNRAIRE
RSQPPHDLLG SIVEGSNPNA PSWRHILRMS ESPWTRDHAI QSNVIYPAAG YICLAIEASR
QLHVLNQTAG EIGGYRLRDV DFLQALMIPD SSDGIEIQTT IRPVSEKDIA SQGWRHFEVW
SVTTDNRWTQ HAKGLVSVEL GESSVRMSRP ARKNITGYTR RILPADLFAN LRNLGITHGP
VFQNMDSIIQ SGSEMRSVVS MTLPDVSVPN DLPRNHILHP VTLDSVITAP YSAVPGAAAR
EITAKVPRSV ERFWVSSKIS HDAGHSLEAD TTLIRDDDQG MAADVLVSDH DTGNIMLEMN
GFSYQSLGRS TSLQKSESWP NELCNKVVWS LDISTPLPAT LAAVRNELAC TVQSAECDTT
KATLRACIYF MQLALVALDS HDIAEMEQHN ASYYTWMKDT VELASSGKLF EGSAEWLYHS
ENERQLHIEQ VQTRLDGEIV CRLGTQLVDI LRGHTGALDL VMQDNLLSRF YSYAPRWKRA
GTQIAGLLRH LSHKNPRARI LEVGAATGAI ALHALGALGT SDSGGPNASM YHFTDTSTAL
FETARESLQP WADLLSFDEL DIEHDPASQG YTPGTYDIVI ASNIRSISES TSQALSNISS
LLKPGGTLLL VEPLKYEVDV HFVRRLLPGR WWDDSTELKA NLCLDMPSWE NQLLSAGFTG
VELELLDRED PQEAALVTFM STVQLPQPPK SNVDADQVVI VTSRNGCPPA AWVKGLKDAI
AAYTVSEGKL GPIVQDLESL AATAASYADK ICIFLGEVDE GILYNLNSTL LEGIRSMSTN
SKGLIWVTRG GAVDCERPEM SLATGFIRSL RNEYVGRKLL TLDLDPKGTP WSDVSMAAIA
KILGTVIGNS AGGSMVEKGA VELEYAERDG VILIPRIYHD VTRNRMLSPD ASDAAMEKIS
IENFYQPTRP LCLKPDLLVF GDDDFSADYL EHLPPASLEV QPKAYGATLN SVGDHIAGFE
CAGIITQVGE EAAAQGYAVG DRVLSVLRHS SFPSRAVVDW KLTTRMPTDM TFQEGASLPL
SFLSAYFALV EIARLQRSRS VLIHAGAGDV GQAAIMVAQH LGAEVYVTVG SPAERGLLIL
KYGLPADHIF SCTDLSLANA VVAATQGRGV DVVLNSLTGP LFQESLNLVA PLGHFVEIGR
RNTQTNGYMH MRPFDRGISF ATLDIPSLLE YRAMDVHRCL AELTRLIELK AVTPVHPITF
HAIGEIAEAS RLLKAGDQIG KVVLSVDEHS TVTAVPSKPA AKLSSEVSYL IVGGSGGLAQ
SVAHWMVNRG ARNLVLLSRS AGTSEKTAAF AEDLRQAGCR RVLPISCDVA NEESLGDAIN
QCAQEGLPPI RGIIHAAFVL RDAFVEKMTL DDWTYTIQSK VAGTWNLHNQ FNLPGDLDFF
VLFSSINGIL GYASQSAYSA AGAYEDALAH WRVKHCGLPA VSIDLSVVNA VGYVAEANAS
ETLRRSLLRA GRRVIDEDHV LGSLESAILS PFDPQFVVGG INSGPGPHWD LDGDLGRDMR
VLPLKYRPPA VTGQSQDDDS SSDSLAAKMI ACESQGDAVR VVGTAIAEML AEMFLVPIED
VDLGQSPSQQ GVDSLVAVEV RNMLFSQAGA EVSIFNIMQS PSLTQLAIDV VDRSAHVKLA
G
//
