PKGA_EMENI
ID PKGA_EMENI Reviewed; 1870 AA.
AC Q5AXA9; C8VB30;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Non-reducing polyketide synthase pkgA {ECO:0000303|PubMed:22510154};
DE Short=NR-PKS pkgA {ECO:0000303|PubMed:22510154};
DE EC=2.3.1.- {ECO:0000269|PubMed:22510154};
DE AltName: Full=Pkg biosynthesis cluster protein A {ECO:0000303|PubMed:22510154};
GN Name=pkgA {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_07071;
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, 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).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the pkg gene
CC cluster that mediates the biosynthesis of dihydrocitreoisocoumarin and
CC 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin (PubMed:22510154). The non-
CC reducing polyketide synthase pkgA performs the condensation of one
CC acetyl-CoA starter unit with 6 and 5 malonyl-CoA units, respectively
CC (PubMed:22510154). As pkgA lacks a releasing domain, the thioesterase
CC pkgB is necessary to break the thioester bond and release
CC dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin
CC from pkgA (PubMed:22510154). {ECO:0000269|PubMed:22510154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + holo-[ACP] + 6 malonyl-CoA =
CC 3,5,7,9,11,13-hexaoxotetradecanoyl-[ACP] + 6 CO2 + 7 CoA;
CC Xref=Rhea:RHEA:64484, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:15846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:142800; Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64485;
CC Evidence={ECO:0000269|PubMed:22510154};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 5 H(+) + holo-[ACP] + 5 malonyl-CoA = 3,5,7,9,11-
CC pentaoxododecanoyl-[ACP] + 5 CO2 + 6 CoA; Xref=Rhea:RHEA:64488,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16607, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:155859;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64489;
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: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22510154}.
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 an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000305|PubMed:22510154}.
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DR EMBL; BN001304; CBF79143.1; -; Genomic_DNA.
DR RefSeq; XP_664675.1; XM_659583.1.
DR AlphaFoldDB; Q5AXA9; -.
DR SMR; Q5AXA9; -.
DR STRING; 162425.CADANIAP00000398; -.
DR EnsemblFungi; CBF79143; CBF79143; ANIA_07071.
DR EnsemblFungi; EAA61200; EAA61200; AN7071.2.
DR GeneID; 2869980; -.
DR KEGG; ani:AN7071.2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_1_1; -.
DR InParanoid; Q5AXA9; -.
DR OMA; FANVVDY; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
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 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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1870
FT /note="Non-reducing polyketide synthase pkgA"
FT /id="PRO_0000450874"
FT DOMAIN 1795..1870
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:22510154"
FT REGION 40..279
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 419..841
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 453..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1282
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 1004..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1704
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT COMPBIAS 453..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1832
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1870 AA; 203487 MW; 02B947423124F4BB CRC64;
MTPSASPSPS PNPGDANVKV DADSPNDFIL FSHELPSGDI QDLIRRLHRY GTLPGYPHLA
RFLQECALLL RTEIQKLPRA LRDSVPPFHD VVTLASHWDR LKSGPLSGAW DGPFLCLYEI
AMLIGHHETH QLSYRRPACL VGISVGLFSA AAVAVSKSIS DLVSYGAESV RTAFAFCVHV
QRVSQELEPT MTEQAASVSW ATVVIGVPAD TIQVELDRFN HLKESESPGA NARPLTGVSI
SHVDQTSVGV TGPPSRLKQL FRQSELLRSS RHSALPISGG LCHVPNVYDD EDVRAILEMA
EVWEKWGTRA LQVPLISPFT GSPFLCPDAY HLIEAICTEA LTKQLYFDKL AGGVVTQLNG
LSCQVLHYGA SLMSDTIIDD VTSQLSPCDT ARQCLVDWAL RDAFDQLPGG PTPPRDAKLA
VVGMACRMPG GADTPDHFWE LLMNGVDTHT TVPPDRFDLD AHFDPSGEKE NTTTKGSQSN
RPLSRQAEQT DPMQRLALVT AYEALEMAGF VPNRTPSSHL SRVGTYYGQA SDDYREVNAG
QKIGTYGIPG TERGFGNGRI NYFFNFQGPS FNIDTACSSG LAAVQAACSA LWAGEADTVV
AGGLNVITSP DIYCMLSKGH FLSKTGQCKV WDIGADGYCR ADGIGSVVIK RLDDALADND
VILACISAGA TNHSAESISI TQPHAAAQRE NYRQVMDRAG VSPLDVSFVE LHGTGTQVGD
AVESESVLSF FAPLGRRSHP DKRLHLGAVK SNIGHGEAAA GIASLIKVLL MYRNNTIPRH
IGIRTAMNPV VAQHLANRNA GILSENHPWL AATASKKRYA IVNSFGAHGG NTTLLLEDAP
SQHSQRYKNH SRRVVASSEV VCTSAKSKAS LRANIRALLA YLDTHQETDL RDLAYTTSAR
RMHHHIRIAS SVTSTAQLRS FLQAAADDVD AYAKHIATAT KRTAVFAFSG QGCLYHGAAA
HLFEQAPLFR NQVLQLDRIV RRLGFPSILV TVAGDAASVY DSARCPHRES TPSSDASHDS
NTNRTSTAPA VDSPLIAQLA LVVIQIALVQ YWGLLGIKPS VVIGHSLGEY AALVAASVLS
VADALFLVGK RAELMLAVCE PGSHAMLSVR GASVDRIEEL CRESEKRYPF EVSCVNGLTD
LVVTGLRGDM ASLRDLLQGS GLKCVLLDIP FAFHSKQMSP ILEDFENAAQ QITFQEPAVP
VISPLLGKCI SEANVINGKY LARATREPVD FVAALDSAWA DGTVNDKSIW IDIGPHPVCT
SFASNHYGKA ATQSFASLRR GDETLSTLTA TLAALHCLGL PVDWNEYYDL RENPARLLHL
DSYQWNYKNY WIPYEGSWTL DKAHAGQNNK TKDDNSAVTP AFFTSSVQQI IFEEYDESMG
RMEALSDLHH PDLQGAADGH KIHGRSVVTG SIWADITLTV GEYLYKQMVP GGKMPHMNVK
GMEVLEAQVL HPDMSQFIQI EGVLDLPRQQ TAVRLYAASA NGTRNTDKPF ASATVCYEEA
QDWQDQWQMT SHLVAARANS FWEMAAGGSD DNARPAGKGG PRVNNFFRSI AYQLFANVVD
YGARYRGMQR VALSEDTLEA TADIVLDKDR HGTWHTPPHW IDSAFQLAGF VMNSFGVQGD
GKISGSSRDF FYITPGWRHF RLLERLEPGP EATYRSFVRM FPVGSEPGAY SGDIYLHRGK
RLVGVCAGIK FKAVPRALMP VLFPRIEPQA GKRRNQAQTA ENRLVKGKGN CEYTHTVFQE
PKSRTPAYDV TKSQPHAEHC DISISQKTQP VAAVPVTQPA LPAKERGEQN QGQSQSQNAQ
ATACLSLISD ETGLDLDDLT GEAAFADLGV DSLMSLALSA KIRAELGIDV QSSIFLECPT
VQDLVTWLSK
