SORB_PENRW
ID SORB_PENRW Reviewed; 2664 AA.
AC B6HN77;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Non-reducing polyketide synthase sorB {ECO:0000303|PubMed:25580210};
DE Short=NR-PKS sorB {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:25580210};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein B {ECO:0000303|PubMed:25580210};
GN Name=sorB {ECO:0000303|PubMed:25580210}; ORFNames=Pc21g05070;
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.
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: Non-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,
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:G0R6S9, ECO:0000269|PubMed:25580210,
CC ECO:0000269|PubMed:28618182}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000255};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25580210}.
CC -!- DOMAIN: Multidomain protein; including an N-terminal starter unit:ACP
CC transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a
CC malonyl-CoA:ACP transacylase (MAT) domain, a product template domain, a
CC acyl carrier protein (ACP) domain, a methyltransferase domain and a
CC reductive NADPH-binding domain that is required for NADPH-dependent
CC product release. {ECO:0000305|PubMed:25580210,
CC ECO:0000305|PubMed:28618182}.
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DR EMBL; AM920436; CAP95404.1; -; Genomic_DNA.
DR RefSeq; XP_002567553.1; XM_002567507.1.
DR AlphaFoldDB; B6HN77; -.
DR SMR; B6HN77; -.
DR STRING; 1108849.XP_002567553.1; -.
DR EnsemblFungi; CAP95404; CAP95404; PCH_Pc21g05070.
DR GeneID; 8313804; -.
DR KEGG; pcs:Pc21g05070; -.
DR VEuPathDB; FungiDB:PCH_Pc21g05070; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR OMA; MGMEMAR; -.
DR OrthoDB; 13314at2759; -.
DR BioCyc; PCHR:PC21G05070-MON; -.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR041068; HTH_51.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2664
FT /note="Non-reducing polyketide synthase sorB"
FT /id="PRO_0000443836"
FT DOMAIN 1711..1785
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..281
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT REGION 431..852
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 961..1276
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1376..1548
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1789..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2197
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000255"
FT REGION 2281..2526
FT /note="NADPH-binding (R) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1789..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Nucleophile; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 302
FT /note="Proton donor/acceptor; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1745
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2664 AA; 292038 MW; 1F025CFD11F465EA CRC64;
MAENSGRGYQ TPVHRDVFFS KSAPQSGNTA DDIPNAASQP DTTSTMAMPS AKTLLLFGPG
AMSLDQTYFS RILSFVKDDA ASQWAVRAIE DIESGWDALS ESIPKLQQTP GADHARRLAE
WLRTGVITPR TTVANLPNAI LGPLVIIAQL VEYLQYVESS QSANGDGKLF QLPSTAQTET
VGCCLGVFSA LVVSSSSSWA KFHHNAAAVL RKVFVLGALS DAQDISDVTG SSVSLIAFWR
GGQSLSDLKK VLEICPGAYI SVLYDDNRAT VTTPSRIASD LKGHLSRAGF TASETEFHGR
FHAGELYNND LEALFSFCRK DPLFQLPDAS SLILRTRVNS EKILADNDSL LEVASRAFLV
EQFNWVKTFR SAVSSSLQDR TSKVIEFGPE RCVPPTLLRR LNSQVTHYEF QSTGQRHSNP
DMPSGCIDND IAVIGMSCQV AGAQDLEQYW NILLEGRSQH KNLVPNERFA METVFRPGQD
GEDRKWYGNF IDDYDAFDYK FFRKSPREVL HMDPQQRLIL QTAYQAVAQS GYYHRPGADR
RIGCYIGCVA NDYENNISHT SPTAFSATGA LRSYIAGKVS HYFGWTGPGM MLDTACSAST
VAIDLACRAI LSGDCSAALA GGTNFYSTPM FFQNLAAGSF LSPTGQCKPF DAKADGYCRG
EAIGAVFLKK LSNAIADGDQ ILGVISATAI NQNQNDTPIF VPNPSSLTNV FQNVVGKAGL
EVNDISVVEA HGTGTPVGDP AEYDSIRQVF GGSVRAGLKP LQLGSVKGLI GHTEGASGVV
ALIKMLLMMQ ESRIPPQASF TSMSASIKAS PADNMEITKA ALPWEDESKV ALINNYGAAG
SNASMVIKQA PKYPSGSEAV GHGSADLTSP TSTFRCPFYI SGLDDKAIRA YATRLRQFIK
NKVISRDVLG IENLSFNVNR QSNWSLSRGF VFGAESITEL EEKLASFETF AVPSVRPVIL
CFGGQVSKSV GLDRGVFDKA TVLRKYLDRC DSVCKSIGAG SIYPGIFQSE PILDPAVLQP
LLLSMQYSCA LSWIDCGVEP AALVGHSFGE LTALCVSGIL SLEDALKLVH GRSKIIKESW
GPEKGSMIAV EADRNDVEKL LVASNARLGE TERAGHATIA CFNGPKSFTI AGSAAAIDAV
QQTVSTLDIP IKHKRLDVTN AFHSTLVEHL RPQLEALGRS LSFGNAHIPL ERATEQRETG
PISPAYVAEH MRNPVYFDHA VQRLASQYPE AIWLEAGSNS TITTMTGRAL GMPKGSTFQP
VSVTGTTQGT RQLADVTMSL WNAGLPCSFW PHSRAQTYGY APIMLPPYQF EKYRHWLEFK
PPPKPVVIER LVYENGGVDQ EAPAPGLYTF MGYGDKTETD CRFRINTTTK SYVDIVSGYT
LGKTVQACPP IFGIDTAIQA ITSVRLEVIA ANELHPHIYN VLNHLPLVMD PTRAVFLEFE
RSGHAPEGWK FKLTSEADDS SKTVHLSGQL EFHRADDARS NFEFSRLERL VTHERCLRAL
ESADDADEVI QGQSIYKVYS DLVSYAPKFR GLQRLVGRPS ESAGRAVKRR SRDSWLDFAL
GETFSQVGSI WVNCLAPGRN TADDTVYIAD GIEQWMRSPS LLRKISEGSY ADHQSEWQIL
ATHKRTEGDT FITDIFVFDS ASRLLDEALL GVKFSARSMS ELFTNVVIAA PPVPFPATIA
PISSAPTENQ YSSMTTSPPA RAQVQKRNTK TELWAKLLPV LADISGLEPE EINETDALAD
IGIDSLMGME MAREVETTFN CTLEQSELMS IFDVPGILAF LQSTLGLEGE DDASQSSDAA
SSSRNTPPSS NDGILATPSP KLEEEDISRS YIDLGNEVGL PAFAVIEAFR AANEQTDAYL
KKWKCAGYLD GASQKQTRLC LVLTSDAFKQ LGCDLVAAKP GEVLQPVPFV PRHHRFHEYL
YKMLEETRII DVDEGIITRT ALPLPTQSSQ AILDDLMSHH PDDGPSHQLT YNIGSRMADV
LSGKADGPQL IFGDAKNREL VAAFYGELPF NKLYFQLMAD FLSRIAESLR LCAQNRGPLK
ILEMGAGTGG TTKVLVPALA KLGIPVEYTF TDLSPSLVAQ AKKKFKQYPF MKFAVHDIEQ
PPSDPLLIGS QNIVIASNAV HATHSLQVST QNIRKFLRPD GFLMLLEMNS TLHWVDVVWG
TLEGWWLFED GRTHAVVDER QWEKELLDAG YKHVEWTDGK LPEVRVQRVR IALADDVEQN
VGRLPPVAKQ QVDDHDLSEE ELNEKKQVAD DYVKETIRGF TIPAYSGDLT DSSEYGKAVL
VTGTTGSLGS HIIAHLVSLP SVDRVYCLNR PAIGGARAKD ATPRDPLHRQ LQSLESKSIA
LDASQLAKLK VIETDSSKAQ LGLDTEEYKH LLCHVTHIIH NAFPVNGLRS LKQNEAQFTI
MRNLVDLAAE ISARRKATDF KFAFQFISSL SAVGKYPSVH AGEIQVPEEH LNIDSALPNG
YGGAKVICER ILHETLGQYP ERFRAMTVRL GQLSGSMETG YWNHMEVLGF LFKSAQTLRS
FPAVEGILTW LPLEQASATL ADLLLRDAPD CHPVYHVDNP VRKPWAEIVP VLAQALGIPE
KGIVPLDDWL RRVKAFPGED PWDNPAGKAI DFFEHKFQHM SCGGVTMATN NAVEHSPTLR
GVQPVADAVV MKYFQVWKDT GFLR
