PKBA_EMENI
ID PKBA_EMENI Reviewed; 2517 AA.
AC Q5AZ32; C8V0D5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Non-reducing polyketide synthase pkbA {ECO:0000303|PubMed:22510154};
DE Short=NR-PKS pkbA {ECO:0000303|PubMed:22510154};
DE EC=2.3.1.- {ECO:0000269|PubMed:22510154};
DE AltName: Full=Cichorine biosynthesis cluster protein pkbA {ECO:0000303|PubMed:22510154};
GN Name=pkbA {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_06448;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP DOMAIN, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=22510154; DOI=10.1021/ja3016395;
RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT nidulans.";
RL J. Am. Chem. Soc. 134:8212-8221(2012).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=24244835; DOI=10.1039/c2md20055d;
RA Sanchez J.F., Entwistle R., Corcoran D., Oakley B.R., Wang C.C.;
RT "Identification and molecular genetic analysis of the cichorine gene
RT cluster in Aspergillus nidulans.";
RL Med. Chem. Commun. 3:0-0(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, BIOTECHNOLOGY, AND PATHWAY.
RX PubMed=30708999; DOI=10.3390/molecules24030515;
RA Liao L., Zhang X., Lou Y., Zhou C., Yuan Q., Gao J.;
RT "Discovery of three new phytotoxins from the fungus Aspergillus nidulans by
RT pathway inactivation.";
RL Molecules 24:0-0(2019).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of cichorine, a phytotoxin active
CC against knapweed, corn, and soybeans (PubMed:22510154, PubMed:24244835,
CC PubMed:30708999). The first step in the pathway is performed by the
CC non-reducing polyketide synthase pkbA that condenses one acetyl-CoA
CC starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also
CC catalyzes one methylation step to produce 3-methylorsellinate
CC (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB,
CC the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE
CC are involved in the conversion of 3-methylorsellinate into nidulol
CC (PubMed:24244835). CicB converts 3-methylorsellinate to a yet
CC unidentified intermediate, cicH may play a ring-closing role for
CC cichorine and cicE is plausibly responsible for the methylation of one
CC of the phenol groups (Probable). The oxidoreductase cicC acts
CC downstream with still unidentified enzymes to further convert nidulol
CC into cichorin (PubMed:24244835). {ECO:0000269|PubMed:22510154,
CC ECO:0000269|PubMed:24244835, ECO:0000269|PubMed:30708999,
CC ECO:0000305|PubMed:24244835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H(+) + 3 malonyl-CoA + S-adenosyl-L-methionine =
CC 3-methylorsellinate + 3 CO2 + 4 CoA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:64500, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:146372;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64501;
CC Evidence={ECO:0000269|PubMed:22510154};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:22510154,
CC ECO:0000269|PubMed:24244835, ECO:0000269|PubMed:30708999}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and 2 acyl-carrier proteins (ACPs) that
CC serve as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000305|PubMed:22510154}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cichorine.
CC {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:24244835}.
CC -!- BIOTECHNOLOGY: Cichorine and its derivatives are promising in the
CC course of developing novel herbicides. {ECO:0000269|PubMed:30708999}.
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DR EMBL; BN001301; CBF69451.1; -; Genomic_DNA.
DR RefSeq; XP_664052.1; XM_658960.1.
DR AlphaFoldDB; Q5AZ32; -.
DR SMR; Q5AZ32; -.
DR ESTHER; emeni-q5az32; Hormone-sensitive_lipase_like.
DR EnsemblFungi; CBF69451; CBF69451; ANIA_06448.
DR EnsemblFungi; EAA58470; EAA58470; AN6448.2.
DR GeneID; 2871344; -.
DR KEGG; ani:AN6448.2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_3_1; -.
DR InParanoid; Q5AZ32; -.
DR OMA; GACTWLE; -.
DR OrthoDB; 93381at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0062032; P:cichorine biosynthetic process; IDA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 3.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
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; 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; IPR001375; Peptidase_S9.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF07859; Abhydrolase_3; 1.
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; PF00326; Peptidase_S9; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..2517
FT /note="Non-reducing polyketide synthase pkbA"
FT /id="PRO_0000450873"
FT DOMAIN 1574..1651
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1685..1761
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 59..250
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 383..748
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 849..1158
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q0CRQ5, ECO:0000255"
FT REGION 1251..1525
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q0CRQ5, ECO:0000255"
FT REGION 1659..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2075
FT /note="Methyltransferase (CMeT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q0CRQ5, ECO:0000255"
FT REGION 2200..2514
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000250|UniProtKB:Q0CRQ5, ECO:0000255"
FT ACT_SITE 547
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 935
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1611
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1721
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2517 AA; 274132 MW; B36422F0A1AC0C7C CRC64;
MAPAPSALVF GSQTTLPSVE AASRLRAALL LDPRLYRMRT SIESLPEIWP ALAISDPALE
RVAGPAEKSL RQLCRWLSHS EFPDATEISE LPATFVTPFT VILHTVLYMH YTDENGSRGH
ADVLRAVRNN GGVQGFCTGF LTAVSVATSP DLEALSRQAS VALRLAVAIG AYIDLDLLDS
DVSSVAVRSR AGKKGLEETL AQFPGAYISV ITDELNATVT APRASLDALS QSLASNGLSA
KRFDLRGRFH HPAHQKALEG LYNLVASNPV FQFSHSELLA PVYSNIDGQL LSSDSIIDTL
LQSILVQRCD WYASISTALH KRSNGEKTSV VQFSLVECIP PSVLRQARLS VQRITDVPVQ
NSPATVPAPL NAVRARIQTS EPIAIIGMGC KFPGADTLDE YWQLLAQGTS MCRTMPEERF
KTSSLRRSPG EKLKFWGNFV NDVDAFDHRF FKKSSREAAS MDPQQRLVLQ VAYQTLESAE
YSGLSGIKAS RDVGCYLGLC ASDYTDNVAS HPPNAFSSLG TLRAFLSGKI SHFFGWTGPS
ITYDTACSSS AVAIQAACRA LQTGECSMAL AGGVSLYTSP NFYQNLSAAS FLSPTGPTKP
FDAKGDGYCR GEGVGLVFLK PLSSALADHD NIMGVIAAAA VNQNQNSTAI TVPHSESQIE
LYRKVVSEAG LHPHDVSFVE AHGTGTPVGD PIEFTSIRTV FGGSNRANPL AIASVKGNIG
HTEGAAACIN NYGAAGSNAA MIVTEAPTGA RSEKQGTLPK CPIYVSANTV SSLKEYCKEL
LRSLRGRSPD CLASLAFQLA NSQNRGFPHA LITSVTSKAE LEDQLSAVVE NRNNSLHTVA
PTERPVVLAF GGQVARSVGL SRQVYDSSAV LRTHLSNCDD ILTSAGLNSI FPAIFRKEPI
ADVVLLHSAL FSAQYACAMT WIEAGVIPAA LIGHSFGQLT ALSVGRVLSL KDGLGLITER
AKLMRDAWGP EHGSMVSVQA DVQTVARLMK AAETKDPKDA LEIACFNGPT SHVVVGSADA
ADRLEAALTQ ESIRYKRLAV SHGFHSKFTE PLLLGLEQCA ERLTFRTPKY AIETCSSGSS
WSEFNASMIV QHTRTPVYYT EALARIEAKL GACTWLEVGT GGSVAGMIRG ALNVPSDHLI
QAVNLAGETG TAALADATVN LWKSSHKLQF WAFHRSEREC YQPLELPPYQ FEKTRHWLDW
KDTMTEQATV TQSTREETSV EEFLTFVKYK DSTKQQAEFR ISTEHEKYSF FVKGHAVLAE
PLCPAPLYID LACKAGQMVY SDTSETLIIP SVEDLEIQAP LGVGDRVIIL RLQQSPFLKT
AWTFCFCSRP VMGNSAEEQL HASGTVVLRE NDTKTAAEFS RFGRLVSSKR VQEMKSDPDC
HILQGPVVYQ LFSRVVSYAD YYKGVQSVYA SGAEVTGRIR LPPTVKDADT RRPLLVDNFI
QTAGIHVNCL TDVGAKEVYV CTKVDRVQSA AAFTEDLANV DASWIVHSSY HPTSEKEVVN
DIFVFNAATG ELAMFILGAH FTRVQISSLG RVLSRANTAD AAPIKVAVPV QSPALRAQPK
RVLLPPLTKR SITRPTLEIS EKLKKTLSRV VEVPVADIHD GGILADLGVD SLLGTEVLTE
INQVFNVSIP ADEFALLTDV ASISKCLASY LGVHDSGSQP EDLADADSVE SDSDMPTGAV
TSGITTPDDA VSRLADLLAE NLEYDGTIEA SNNLADLGLD SILSIELAND IKKIFNCDVD
MSQLNMESTF ADLIALVPAL NIEQSLSSVP ASLTTQGSDF EMAQHAFEQI RFDYDIYTKE
TGFYDFWKRV YPAQSRLVLA YTVEAFAQLG CDLALMHPGD RLPKIGYLPA HEKLVQQLYN
ILRDGMLVAT SDSGFVRSDK PVDPTSSTRL LEEINTIAPQ HASEHSLLHI TGSKLADCLT
GTADPLNLLF RSKANRDLLA EVYLNGPMYA AISRLLCSFL GNAFSDRQSS GTFQILELGG
GTGGTTGHVL DYLVRSGIPF TYTFSDVSGS FVAAARKKFA GRPYMEYQVI DIEKEPADSL
TGKFHAVIST NCIHATTNLE ISTGNIHRML RPDGFVALVE FTRNMYWFDL VFGLLEGWWL
FEDGRQHVIA SESFWNTSMR KAGFQHVSWT DGDSFEARTL RIIAGFRAPA VNEIYTPRLD
SRDTETAVES VMYKQADGIP LFADIYYPPS VSNEPRPIAL MIHGGGHIML SRKDIRPKQT
AHLHTLGFLP VSIDYRLCPE TTLTEGPMRD VSDAMAWARS TLCSLPLLCP GLTLDPSRVV
VVGWSTGGHL AMTTAFTSIE RGLSPPDAIL AFYCPTDYED RVWTQPNYPE NTDVDGLSLM
KYNLLEGVQD RPITAYNIPL TSRSNSKAGG TPAGGWMAPD DPRSRIVLHM NWKGQCLPVL
LRGLPPSNSL SPGDAEKLIS QPQPEIEEIQ RVSPYAQIRR GVYRTPTFVI HGTDDDLIPY
EQSVRTVQAL KDMGVRAEVS VPQGKAHLFD MFKDADGSSW EVVKRGYDFL KEEVSGK
